7TZO: The apo structure of human mTORC2 complex

The apo structure of human mTORC2 complex. Determined by electron microscopy at 3.28 Å resolution. Released 11 Jan 2023.

Method: Electron microscopy
Resolution: 3.28 Å
Organism: Homo sapiens
Chains: 8
Atoms: 57,117
Mol. weight: 1189.81 kDa
Released: 11 Jan 2023

Explore 7TZO in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7TZO contains 464 α-helices and 94 β-strands across 8 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 141 helices, 14 β-strands

Element	Residues	Length	Sheet
α-helix	19-28	10
α-helix	38-46	9
α-helix	47-51	5
α-helix	62-72	11
α-helix	84-92	9
α-helix	102-113	12
α-helix	122-133	12
α-helix	141-144	4
α-helix	146-149	4
α-helix	151-154	4
α-helix	165-177	13
α-helix	183-185	3
α-helix	190-196	7
α-helix	197-199	3
α-helix	205-222	18
α-helix	234-243	10
α-helix	262-275	14
α-helix	278-286	9
α-helix	363-374	12
α-helix	387-402	16
α-helix	412-423	12
α-helix	430-443	14
α-helix	445-450	6
α-helix	452-456	5
α-helix	459-461	3
α-helix	480-490	11
α-helix	500-502	3
α-helix	506-510	5
α-helix	515-527	13
α-helix	532-543	12
α-helix	544-548	5
α-helix	581-589	9
α-helix	600-605	6
α-helix	609-612	4
α-helix	616-628	13
α-helix	649-664	16
α-helix	669-678	10
α-helix	681-686	6
α-helix	690-700	11
α-helix	705-719	15
α-helix	723-743	21
α-helix	747-763	17
α-helix	769-771	3
α-helix	772-783	12
α-helix	793-808	16
α-helix	817-828	12
α-helix	837-851	15
α-helix	857-860	4
α-helix	864-874	11
α-helix	878-891	14
α-helix	896-901	6
α-helix	928-936	9
α-helix	943-945	3
α-helix	947-960	14
α-helix	968-982	15
α-helix	983-989	7
α-helix	994-1003	10
α-helix	1008-1020	13
α-helix	1028-1040	13
α-helix	1048-1063	16
α-helix	1067-1070	4
α-helix	1072-1074	3
α-helix	1075-1083	9
α-helix	1088-1090	3
α-helix	1091-1101	11
α-helix	1104-1106	3
α-helix	1111-1121	11
α-helix	1129-1142	14
α-helix	1153-1162	10
α-helix	1169-1183	15
α-helix	1186-1191	6
α-helix	1192-1200	9
α-helix	1207-1217	11
α-helix	1229-1237	9
α-helix	1264-1268	5
α-helix	1277-1293	17
α-helix	1298-1307	10
α-helix	1311-1316	6
α-helix	1318-1326	9
α-helix	1331-1347	17
α-helix	1351-1365	15
α-helix	1372-1373	2
α-helix	1377-1379	3
α-helix	1380-1389	10
α-helix	1393-1406	14
α-helix	1410-1422	13
α-helix	1426-1435	10
α-helix	1436-1440	5
α-helix	1448-1453	6
α-helix	1456-1468	13
α-helix	1478-1487	10
α-helix	1491-1500	10
α-helix	1506-1523	18
α-helix	1526-1533	8
α-helix	1541-1553	13
α-helix	1559-1579	21
α-helix	1583-1597	15
α-helix	1599-1607	9
α-helix	1612-1623	12
α-helix	1630-1640	11
α-helix	1650-1663	14
α-helix	1666-1677	12
α-helix	1688-1689	2
α-helix	1694-1707	14
α-helix	1712-1730	19
α-helix	1740-1762	23
α-helix	1768-1783	16
α-helix	1787-1807	21
α-helix	1874-1895	22
α-helix	1900-1913	14
α-helix	1917-1929	13
α-helix	1933-1938	6
α-helix	1939-1943	5
α-helix	1951-1967	17
α-helix	1970-1980	11
α-helix	1985-1998	14
α-helix	2004-2020	17
α-helix	2023-2041	19
α-helix	2044-2058	15
α-helix	2065-2090	26
α-helix	2097-2112	16
α-helix	2115-2117	3
β-strand	2120-2122	3	1
α-helix	2123-2126	4
α-helix	2138	1
β-strand	2139	1	2
α-helix	2140	1
β-strand	2152	1	2
β-strand	2153-2156	4	3
β-strand	2159-2162	4	1
β-strand	2170-2171	2	1
β-strand	2173-2176	4	3
β-strand	2181-2183	3	3
β-strand	2184-2188	5	1
α-helix	2193-2210	18
α-helix	2213-2216	4
β-strand	2227-2231	5	1
β-strand	2234-2238	5	1
α-helix	2239-2240	2
β-strand	2243-2245	3	4
α-helix	2246-2256	11
α-helix	2263-2271	9
α-helix	2275-2277	3
α-helix	2280-2291	12
α-helix	2298-2305	8
α-helix	2310-2334	25
β-strand	2344-2347	4	4
β-strand	2353-2355	3	4
α-helix	2381-2385	5
α-helix	2395-2409	15
α-helix	2411-2422	12
α-helix	2495-2509	15
α-helix	2521-2532	12
α-helix	2535-2538	4
α-helix	2543-2545	3

Chain B: 143 helices, 14 β-strands

Element	Residues	Length	Sheet
α-helix	20-29	10
α-helix	39-51	13
α-helix	61-73	13
α-helix	84-93	10
α-helix	102-112	11
α-helix	123-133	11
α-helix	134-136	3
α-helix	141-149	9
α-helix	152-155	4
α-helix	167-178	12
α-helix	181-184	4
α-helix	188-196	9
α-helix	197-199	3
α-helix	205-221	17
α-helix	234-245	12
α-helix	259-261	3
α-helix	262-275	14
α-helix	281-285	5
α-helix	286-288	3
α-helix	360-362	3
α-helix	363-374	12
α-helix	387-402	16
α-helix	411-425	15
α-helix	430-443	14
α-helix	447-450	4
α-helix	451-458	8
α-helix	459-461	3
α-helix	480-490	11
α-helix	501-510	10
α-helix	515-527	13
α-helix	532-547	16
α-helix	579-591	13
α-helix	600-605	6
α-helix	607-610	4
α-helix	616-629	14
α-helix	649-665	17
α-helix	669-678	10
α-helix	681-686	6
α-helix	690-700	11
α-helix	705-718	14
α-helix	719-721	3
α-helix	723-743	21
α-helix	747-763	17
α-helix	769-771	3
α-helix	772-783	12
α-helix	793-808	16
α-helix	814-816	3
α-helix	817-828	12
α-helix	837-851	15
α-helix	856-860	5
α-helix	864-874	11
α-helix	878-891	14
α-helix	896-901	6
α-helix	930-934	5
α-helix	943-960	18
α-helix	968-982	15
α-helix	985-989	5
α-helix	994-1003	10
α-helix	1008-1022	15
α-helix	1028-1040	13
α-helix	1049-1063	15
α-helix	1067-1074	8
α-helix	1075-1083	9
α-helix	1088-1090	3
α-helix	1091-1100	10
α-helix	1104-1106	3
α-helix	1111-1122	12
α-helix	1129-1142	14
α-helix	1152-1163	12
α-helix	1167-1169	3
α-helix	1170-1183	14
α-helix	1186-1191	6
α-helix	1192-1202	11
α-helix	1207-1217	11
α-helix	1229-1237	9
α-helix	1265-1269	5
α-helix	1277-1293	17
α-helix	1298-1309	12
α-helix	1311-1316	6
α-helix	1318-1327	10
α-helix	1331-1347	17
α-helix	1351-1365	15
α-helix	1371-1373	3
α-helix	1377-1379	3
α-helix	1380-1388	9
α-helix	1393-1406	14
α-helix	1410-1421	12
α-helix	1426-1435	10
α-helix	1436-1440	5
α-helix	1447-1453	7
α-helix	1456-1467	12
α-helix	1477-1487	11
α-helix	1491-1501	11
α-helix	1506-1523	18
α-helix	1526-1533	8
α-helix	1541-1553	13
α-helix	1559-1579	21
α-helix	1583-1607	25
α-helix	1612-1623	12
α-helix	1630-1640	11
α-helix	1646-1648	3
α-helix	1650-1663	14
α-helix	1666-1677	12
α-helix	1688-1690	3
α-helix	1694-1707	14
α-helix	1712-1730	19
α-helix	1740-1762	23
α-helix	1768-1783	16
α-helix	1787-1807	21
α-helix	1874-1895	22
α-helix	1900-1913	14
α-helix	1917-1929	13
α-helix	1933-1938	6
α-helix	1939-1944	6
α-helix	1951-1967	17
α-helix	1970-1980	11
α-helix	1985-1998	14
α-helix	2004-2020	17
α-helix	2023-2041	19
α-helix	2044-2058	15
α-helix	2065-2090	26
α-helix	2094-2112	19
α-helix	2115-2117	3
β-strand	2120-2122	3	5
α-helix	2123-2126	4
α-helix	2130-2132	3
α-helix	2138	1
β-strand	2139	1	6
α-helix	2140	1
β-strand	2152	1	6
β-strand	2153-2156	4	7
β-strand	2159-2162	4	5
β-strand	2170-2171	2	5
β-strand	2173-2176	4	7
β-strand	2181-2183	3	7
β-strand	2184-2188	5	5
α-helix	2193-2210	18
α-helix	2213-2216	4
β-strand	2227-2231	5	5
β-strand	2234-2238	5	5
α-helix	2239-2240	2
β-strand	2243-2245	3	8
α-helix	2246-2256	11
α-helix	2263-2271	9
α-helix	2275-2277	3
α-helix	2280-2291	12
α-helix	2298-2305	8
α-helix	2310-2334	25
β-strand	2344-2347	4	8
β-strand	2353-2355	3	8
α-helix	2381-2387	7
α-helix	2395-2409	15
α-helix	2411-2422	12
α-helix	2495-2509	15
α-helix	2521-2532	12
α-helix	2535-2538	4
α-helix	2543-2545	3

Chains C and D: 1 helix, 28 β-strands

Element	Residues	Length	Sheet
β-strand	14-19	6	9
β-strand	23-28	6	9
β-strand	33-39	7	9
β-strand	47-50	4	10
β-strand	56-61	6	10
β-strand	64-69	6	10
β-strand	79-82	4	10
β-strand	88-93	6	11
β-strand	99-104	6	11
β-strand	108-113	6	11
β-strand	124-126	3	11
β-strand	131-136	6	12
β-strand	142-147	6	12
β-strand	152-156	5	12
β-strand	162-165	4	12
β-strand	173-177	5	13
β-strand	184-189	6	13
β-strand	193-198	6	13
α-helix	199-200	2
β-strand	211-217	7	13
β-strand	223-227	5	14
β-strand	234-239	6	14
β-strand	243-248	6	14
β-strand	254-259	6	14
β-strand	273-277	5	15
β-strand	284-289	6	15
β-strand	294-298	5	15
β-strand	306-308	3	15
β-strand	315-321	7	9

Chains E and F: 83 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	33-45	13
α-helix	46-48	3
α-helix	53-69	17
α-helix	74-77	4
α-helix	81-89	9
α-helix	90-92	3
α-helix	97-110	14
α-helix	114-122	9
α-helix	125-133	9
α-helix	143-157	15
α-helix	163-174	12
α-helix	184-195	12
α-helix	199-204	6
α-helix	208-216	9
α-helix	221-234	14
α-helix	238-241	4
α-helix	250-252	3
α-helix	255-258	4
α-helix	274-291	18
α-helix	295-301	7
α-helix	308-316	9
α-helix	324-335	12
α-helix	337-342	6
α-helix	346-352	7
α-helix	360-362	3
α-helix	364-367	4
α-helix	370-376	7
α-helix	378-379	2
α-helix	387-401	15
α-helix	404-413	10
α-helix	417-437	21
α-helix	440-442	3
α-helix	446-448	3
α-helix	450-456	7
α-helix	463-485	23
α-helix	492-508	17
α-helix	526-534	9
α-helix	548-556	9
α-helix	568-581	14
α-helix	583-585	3
β-strand	592	1	23
α-helix	599-614	16
α-helix	620-638	19
α-helix	648-651	4
β-strand	654	1	23
α-helix	655-658	4
α-helix	659-666	8
α-helix	670-678	9
α-helix	682-689	8
α-helix	696-702	7
α-helix	712-722	11
α-helix	726-734	9
α-helix	737-741	5
α-helix	747-758	12
α-helix	764-777	14
α-helix	781-788	8
α-helix	799-806	8
α-helix	807-810	4
α-helix	812-819	8
α-helix	823-830	8
α-helix	831-835	5
α-helix	836-851	16
α-helix	878-880	3
α-helix	882-886	5
α-helix	887-889	3
α-helix	892-897	6
α-helix	901-910	10
α-helix	917-933	17
α-helix	937-944	8
α-helix	949-958	10
α-helix	962-974	13
α-helix	979-986	8
β-strand	990-991	2	24
α-helix	1002-1004	3
β-strand	1429-1430	2	24
α-helix	1433-1437	5
α-helix	1445-1447	3
α-helix	1481-1484	4
α-helix	1489-1492	4
α-helix	1525-1528	4
α-helix	1531-1535	5
α-helix	1610-1625	16
α-helix	1629-1642	14
α-helix	1644-1648	5
α-helix	1650-1660	11
α-helix	1667-1675	9
α-helix	1683-1693	11

Chains G and H: 6 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	7-20	14
α-helix	26-30	5
α-helix	67-71	5
α-helix	87-100	14
β-strand	104-106	3	10
α-helix	120-123	4
α-helix	140-145	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Serine/threonine-protein kinase mTOR	A, B	protein	2674	Homo sapiens	P42345 (AlphaFold model)
Target of rapamycin complex subunit LST8	C, D	protein	347	Homo sapiens	Q9BVC4 (AlphaFold model)
Rapamycin-insensitive companion of mTOR	E, F	protein	1720	Homo sapiens	Q6R327 (AlphaFold model)
Target of rapamycin complex 2 subunit MAPKAP1	G, H	protein	538	Homo sapiens	Q9BPZ7 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>7TZO_1 Serine/threonine-protein kinase mTOR (chains A, B)
MVTTLSGLSGEQGPSGDMTTEEDSATHIKFSKRDEDGRELAGATMELRDSSGKTISTWIS
DGHVKDFYLYPGKYTFVETAAPDGYEVATPIEFTVNEDGQVTVDGEATEGDAHTGSSGSG
SGTGSMLGTGPAAATTAATTSSNVSVLQQFASGLKSRNEETRAKAAKELQHYVTMELREM
SQEESTRFYDQLNHHIFELVSSSDANERKGGILAIASLIGVEGGNATRIGRFANYLRNLL
PSNDPVVMEMASKAIGRLAMAGDTFTAEYVEFEVKRALEWLGADRNEGRRHAAVLVLREL
AISVPTFFFQQVQPFFDNIFVAVWDPKQAIREGAVAALRACLILTTQREPKEMQKPQWYR
HTFEEAEKGFDETLAKEKGMNRDDRIHGALLILNELVRISSMEGERLREEMEEITQQQLV
HDKYCKDLMGFGTKPRHITPFTSFQAVQPQQSNALVGLLGYSSHQGLMGFGTSPSPAKST
LVESRCCRDLMEEKFDQVCQWVLKCRNSKNSLIQMTILNLLPRLAAFRPSAFTDTQYLQD
TMNHVLSCVKKEKERTAAFQALGLLSVAVRSEFKVYLPRVLDIIRAALPPKDFAHKRQKA
MQVDATVFTCISMLARAMGPGIQQDIKELLEPMLAVGLSPALTAVLYDLSRQIPQLKKDI
QDGLLKMLSLVLMHKPLRHPGMPKGLAHQLASPGLTTLPEASDVGSITLALRTLGSFEFE
GHSLTQFVRHCADHFLNSEHKEIRMEAARTCSRLLTPSIHLISGHAHVVSQTAVQVVADV
LSKLLVVGITDPDPDIRYCVLASLDERFDAHLAQAENLQALFVALNDQVFEIRELAICTV
GRLSSMNPAFVMPFLRKMLIQILTELEHSGIGRIKEQSARMLGHLVSNAPRLIRPYMEPI
LKALILKLKDPDPDPNPGVINNVLATIGELAQVSGLEMRKWVDELFIIIMDMLQDSSLLA
KRQVALWTLGQLVASTGYVVEPYRKYPTLLEVLLNFLKTEQNQGTRREAIRVLGLLGALD
PYKHKVNIGMIDQSRDASAVSLSESKSSQDSSDYSTSEMLVNMGNLPLDEFYPAVSMVAL
MRIFRDQSLSHHHTMVVQAITFIFKSLGLKCVQFLPQVMPTFLNVIRVCDGAIREFLFQQ
LGMLVSFVKSHIRPYMDEIVTLMREFWVMNTSIQSTIILLIEQIVVALGGEFKLYLPQLI
PHMLRVFMHDNSPGRIVSIKLLAAIQLFGANLDDYLHLLLPPIVKLFDAPEAPLPSRKAA
LETVDRLTESLDFTDYASRIIHPIVRTLDQSPELRSTAMDTLSSLVFQLGKKYQIFIPMV
NKVLVRHRINHQRYDVLICRIVKGYTLADEEEDPLIYQHRMLRSGQGDALASGPVETGPM
KKLHVSTINLQKAWGAARRVSKDDWLEWLRRLSLELLKDSSSPSLRSCWALAQAYNPMAR
DLFNAAFVSCWSELNEDQQDELIRSIELALTSQDIAEVTQTLLNLAEFMEHSDKGPLPLR
DDNGIVLLGERAAKCRAYAKALHYKELEFQKGPTPAILESLISINNKLQQPEAAAGVLEY
AMKHFGELEIQATWYEKLHEWEDALVAYDKKMDTNKDDPELMLGRMRCLEALGEWGQLHQ
QCCEKWTLVNDETQAKMARMAAAAAWGLGQWDSMEEYTCMIPRDTHDGAFYRAVLALHQD
LFSLAQQCIDKARDLLDAELTAMAGESYSRAYGAMVSCHMLSELEEVIQYKLVPERREII
RQIWWERLQGCQRIVEDWQKILMVRSLVVSPHEDMRTWLKYASLCGKSGRLALAHKTLVL
LLGVDPSRQLDHPLPTVHPQVTYAYMKNMWKSARKIDAFQHMQHFVQTMQQQAQHAIATE
DQQHKQELHKLMARCFLKLGEWQLNLQGINESTIPKVLQYYSAATEHDRSWYKAWHAWAV
MNFEAVLHYKHQNQARDEKKKLRHASGANITNATTAATTAATATTTASTEGSNSESEAES
TENSPTPSPLQKKVTEDLSKTLLMYTVPAVQGFFRSISLSRGNNLQDTLRVLTLWFDYGH
WPDVNEALVEGVKAIQIDTWLQVIPQLIARIDTPRPLVGRLIHQLLTDIGRYHPQALIYP
LTVASKSTTTARHNAANKILKNMCEHSNTLVQQAMMVSEELIRVAILWHEMWHEGLEEAS
RLYFGERNVKGMFEVLEPLHAMMERGPQTLKETSFNQAYGRDLMEAQEWCRKYMKSGNVK
DLTQAWDLYYHVFRRISKQLPQLTSLELQYVSPKLLMCRDLELAVPGTYDPNQPIIRIQS
IAPSLQVITSKQRPRKLTLMGSNGHEFVFLLKGHEDLRQDERVMQLFGLVNTLLANDPTS
LRKNLSIQRYAVIPLSTNSGLIGWVPHCDTLHALIRDYREKKKILLNIEHRIMLRMAPDY
DHLTLMQKVEVFEHAVNNTAGDDLAKLLWLKSPSSEVWFDRRTNYTRSLAVMSMVGYILG
LGDRHPSNLMLDRLSGKILHIDFGDCFEVAMTREKFPEKIPFRLTRMLTNAMEVTGLDGN
YRITCHTVMEVLREHKDSVMAVLEAFVYDPLLNWRLMDTNTKGNKRSRTRTDSYSAGQSV
EILDGVELGEPAHKKTGTTVPESIHSFIGDGLVKPEALNKKAIQIINRVRDKLTGRDFSH
DDTLDVPTQVELLIKQATSHENLCQCYIGWCPFW

Sequence of entity 2 (C, D), FASTA

>7TZO_2 Target of rapamycin complex subunit LST8 (chains C, D)
MGYPYDVPDYADLNGGGGGSTMNTSPGTVGSDPVILATAGYDHTVRFWQAHSGICTRTVQ
HQDSQVNALEVTPDRSMIAAAGYQHIRMYDLNSNNPNPIISYDGVNKNIASVGFHEDGRW
MYTGGEDCTARIWDLRSRNLQCQRIFQVNAPINCVCLHPNQAELIVGDQSGAIHIWDLKT
DHNEQLIPEPEVSITSAHIDPDASYMAAVNSTGNCYVWNLTGGIGDEVTQLIPKTKIPAH
TRYALQCRFSPDSTLLATCSADQTCKIWRTSNFSLMTELSIKSGNPGESSRGWMWGCAFS
GDSQYIVTASSDNLARLWCVETGEIKREYGGHQKAVVCLAFNDSVLG

Sequence of entity 3 (E, F), FASTA

>7TZO_3 Rapamycin-insensitive companion of mTOR (chains E, F)
MDYKDDDDKGSTMAAIGRGRSLKNLRVRGRNDSGEENVPLDLTREPSDNLREILQNVARL
QGVSNMRKLGHLNNFTKLLCDIGHSEEKLGFHYEDIIICLRLALLNEAKEVRAAGLRALR
YLIQDSSILQKVLKLKVDYLIARCIDIQQSNEVERTQALRLVRKMITVNASLFPSSVTNS
LIAVGNDGLQERDRMVRACIAIICELALQNPEVVALRGGLNTILKNVIDCQLSRINEALI
TTILHLLNHPKTRQYVRADVELERILAPYTDFHYRHSPDTAEGQLKEDREARFLASKMGI
IATFRSWAGIINLCKPGNSGIQSLIGVLCIPNMEIRRGLLEVLYDIFRLPLPVVTEEFIE
ALLSVDPGRFQDSWRLSDGFVAAEAKTILPHRARSRPDLMDNYLALILSAFIRNGLLEGL
VEVITNSDDHISVRATILLGELLHMANTILPHSHSHHLHCLPTLMNMAASFDIPKEKRLR
ASAALNCLKRFHEMKKRGPKPYSLHLDHIIQKAIATHQKRDQYLRVQKDIFILKDTEEAL
LINLRDSQVLQHKENLEWNWNLIGTILKWPNVNLRNYKDEQLHRFVRRLLYFYKPSSKLY
ANLDLDFAKAKQLTVVGCQFTEFLLESEEDGQGYLEDLVKDIVQWLNASSGMKPERSLQN
NGLLTTLSQHYFLFIGTLSCHPHGVKMLEKCSVFQCLLNLCSLKNQDHLLKLTVSSLDYS
RDGLARVILSKILTAATDACRLYATKHLRVLLRANVEFFNNWGIELLVTQLHDKNKTISS
EALDILDEACEDKANLHALIQMKPALSHLGDKGLLLLLRFLSIPKGFSYLNERGYVAKQL
EKWHREYNSKYVDLIEEQLNEALTTYRKPVDGDNYVRRSNQRLQRPHVYLPIHLYGQLVH
HKTGCHLLEVQNIITELCRNVRTPDLDKWEEIKKLKASLWALGNIGSSNWGLNLLQEENV
IPDILKLAKQCEVLSIRGTCVYVLGLIAKTKQGCDILKCHNWDAVRHSRKHLWPVVPDDV
EQLCNELSSIPSTLSLNSESTSSRHNSESESVPSSMFILEDDRFGSSSTSTFFLDINEDT
EPTFYDRSGPIKDKNSFPFFASSKLVKNRILNSLTLPNKKHRSSSDPKGGKLSSESKTSN
RRIRTLTEPSVDFNHSDDFTPISTVQKTLQLETSFMGNKHIEDTGSTPSIGENDLKFTKN
FGTENHRENTSRERLVVESSTSSHMKIRSQSFNTDTTTSGISSMSSSPSRETVGVDATTM
DTDCGSMSTVVSTKTIKTSHYLTPQSNHLSLSKSNSVSLVPPGSSHTLPRRAQSLKAPSI
ATIKSLADCNFSYTSSRDAFGYATLKRLQQQRMHPSLSHSEALASPAKDVLFTDTITMKA
NSFESRLTPSRFMKALSYASLDKEDLLSPINQNTLQRSSSVRSMVSSATYGGSDDYIGLA
LPVDINDIFQVKDIPYFQTKNIPPHDDRGARAFAHDAGGLPSGTGGLVKNSFHLLRQQMS
LTEIMNSIHSDASLFLESTEDTGLQEHTDDNCLYCVCIEILGFQPSNQLSAICSHSDFQD
IPYSDWCEQTIHNPLEVVPSKFSGISGCSDGVSQEGSASSTKSTELLLGVKTIPDDTPMC
RILLRKEVLRLVINLSSSVSTKCHETGLLTIKEKYPQTFDDICLYSEVSHLLSHCTFRLP
CRRFIQELFQDVQFLQMHEEAEAVLATPPKQPIVDTSAES

Sequence of entity 4 (G, H), FASTA

>7TZO_4 Target of rapamycin complex 2 subunit MAPKAP1 (chains G, H)
MAFLDNPTIILAHIRQSHVTSDDTGMCEMVLIDHDVDLEKIHPPSMPGDSGSEIQGSNGE
TQGYVYAQSVDITSSWDFGIRRRSNTAQRLERLRKERQNQIKCKNIQWKERNSKQSAQEL
KSLFEKKSLKEKPPISGKQSILSVRLEQCPLQLNNPFNEYSKFDGKGHVGTTATKKIDVY
LPLHSSQDRLLPMTVVTMASARVQDLIGLICWQYTSEGREPKLNDNVSAYCLHIAEDDGE
VDTDFPPLDSNEPIHKFGFSTLALVEKYSSPGLTSKESLFVRINAAHGFSLIQVDNTKVT
MKEILLKAVKRRKGSQKVSGPQYRLEKQSEPNVAVDLDSTLESQSAWEFCLVRENSSRAD
GVFEEDSQIDIATVQDMLSSHHYKSFKVSMIHRLRFTTDVQLGISGDKVEIDPVTNQKAS
TKFWIKQKPISIDSDLLCACDLAEEKSPSHAIFKLTYLSNHDYKHLYFESDAATVNEIVL
KVNYILESRASTARADYFAQKQRKLNRRTSFSFQKEKKSGQQAAAGGGGYPYDVPDYA

Primary citation

Interactions between mTORC2 core subunits Rictor and mSin1 dictate selective and context-dependent phosphorylation of substrate kinases SGK1 and Akt. Yu, Z., Chen, J., Takagi, E. et al. J Biol Chem (2022) 298:102288-102288. DOI 10.1016/j.jbc.2022.102288 · PubMed

Other PDB entries of the same protein (UniProt P42345 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4DRI 1.45 Å, Co-crystal structure of the PPIase domain of FKBP51, Rapamycin and the FRB fragment of…
9DBO 1.55 Å, Crystal structure of a synthetic Fab (R3E9) in complex with the FRB domain of mTOR
5GPG 1.67 Å, Co-crystal structure of the FK506 binding domain of human FKBP25, Rapamycin and the FRB…
5WBH 1.75 Å, Structure of the FRB domain of mTOR bound to a substrate recruitment peptide of S6K1
4DRJ 1.8 Å, o-crystal structure of the PPIase domain of FKBP52, Rapamycin and the FRB fragment of mTOR
3FAP 1.85 Å, Atomic structures of the rapamycin analogs in complex with both human FKBP12 and frb…
8PPZ 1.85 Å, Co-crystal structure of FKBP12, compound 7 and the FRB fragment of mTOR
8XI9 1.85 Å, Crystal structure of FRB-FKBP fusion protein in complex with rapamycin
9PIW 1.9 Å, Crystal structure of a synthetic Fab (1A) in complex with the FRB domain of mTOR
9DL0 2.0 Å, Crystal structure of a synthetic Fab (R3H8) in complex with the FRB domain of mTOR
9PJ1 2.05 Å, Crystal structure of a synthetic Fab (4R) in complex with the ternary assembly of…
9PIU 2.18 Å, Crystal structure of a synthetic Fab (2C) in complex with the FRB domain of mTOR

Browse structure collections

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