9CAE: PDB entry 9CAE

Cryo-EM structure of the reconstituted RuvBL lobe of the human TIP60 complex (composite structure). Determined by electron microscopy at 3.07 Å resolution. Released 18 Jun 2025.

Method: Electron microscopy
Resolution: 3.07 Å
Organisms: Homo sapiens, Rhodococcus rhodochrous, Escherichia coli K-12
Chains: 12
Atoms: 34,005
Mol. weight: 962.14 kDa
Ligands: AGS, MG
Released: 18 Jun 2025

Explore 9CAE in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9CAE contains 262 α-helices and 255 β-strands across 12 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: 43 helices, 25 β-strands

Element	Residues	Length	Sheet
α-helix	780-791	12
α-helix	795-797	3
α-helix	798-800	3
β-strand	801-802	2	1
α-helix	803-806	4
β-strand	808	1	2
α-helix	811-855	45
β-strand	1319-1326	8	3
α-helix	1330-1341	12
α-helix	1343-1351	9
α-helix	1354-1369	16
α-helix	1371-1373	3
β-strand	1380-1381	2	4
β-strand	1383-1385	3	5
α-helix	1386-1387	2
β-strand	1390-1391	2	6
α-helix	1394-1398	5
α-helix	1404-1406	3
α-helix	1410-1413	4
α-helix	1416-1418	3
α-helix	1424-1432	9
β-strand	1434	1	7
α-helix	1435-1436	2
α-helix	1437-1443	7
α-helix	1460-1463	4
β-strand	1464	1	8
β-strand	1467-1468	2	9
β-strand	1477	1	8
α-helix	1746-1761	16
α-helix	1769-1775	7
α-helix	1825-1829	5
α-helix	1834-1836	3
β-strand	1838-1840	3	5
α-helix	1841-1843	3
β-strand	1845-1846	2	6
α-helix	1852-1869	18
α-helix	1870-1872	3
α-helix	1873-1878	6
β-strand	1885-1886	2	4
α-helix	1887-1889	3
α-helix	1891-1895	5
α-helix	1898-1911	14
β-strand	1917-1921	5	3
α-helix	1924-1936	13
β-strand	1941-1944	4	3
α-helix	1950-1962	13
β-strand	1968-1972	5	3
β-strand	1987-1990	4	3
α-helix	1997-2013	17
β-strand	2016-2023	8	3
α-helix	2028-2031	4
α-helix	2034-2044	11
α-helix	2057-2064	8
α-helix	2189-2216	28
β-strand	2222-2223	2	10
α-helix	2225	1
α-helix	2226-2230	5
β-strand	2232-2236	5	11
β-strand	2242-2244	3	11
α-helix	2245-2246	2
β-strand	2247-2248	2	12
α-helix	2249-2254	6
β-strand	2260	1	2
α-helix	2266-2268	3
β-strand	2270	1	13
α-helix	2274-2276	3
α-helix	2281-2282	2
β-strand	2283	1	14

Chain B: 3 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	211-220	10	15
β-strand	260-264	5	15
β-strand	266-268	3	15
α-helix	271-277	7
α-helix	281-288	8
β-strand	291	1	16
β-strand	298	1	16
β-strand	301-302	2	17
β-strand	309-310	2	17
α-helix	313-330	18

Chain C: 6 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	400-402	3
β-strand	406	1	14
β-strand	412-413	2	1
α-helix	414	1
β-strand	415	1	13
α-helix	416	1
α-helix	428-430	3
α-helix	436-438	3
β-strand	439-440	2	18
β-strand	441-444	4	12
β-strand	451-459	9	12
β-strand	465-469	5	12
α-helix	475-480	6
β-strand	528-529	2	12
β-strand	530-532	3	11

Chain E: 25 helices, 26 β-strands

Element	Residues	Length	Sheet
α-helix	13-14	2
β-strand	15	1	19
β-strand	26	1	20
α-helix	31	1
β-strand	32	1	20
α-helix	33	1
β-strand	35-36	2	21
β-strand	39-40	2	21
α-helix	43-58	16
β-strand	61	1	22
β-strand	65-69	5	23
α-helix	76-87	12
β-strand	93-96	4	23
α-helix	98-101	4
α-helix	108-118	11
β-strand	120-139	20	24
β-strand	157-162	6	24
β-strand	167-172	6	24
α-helix	174-183	10
β-strand	189-194	6	24
β-strand	199-206	8	24
α-helix	207-211	5
β-strand	215	1	15
β-strand	220-221	2	24
α-helix	222-224	3
β-strand	229-239	11	24
α-helix	240-248	9
α-helix	256-262	7
α-helix	265-266	2
α-helix	273-289	17
β-strand	292-296	5	24
β-strand	298-301	4	23
α-helix	304-306	3
α-helix	309-319	11
β-strand	326-331	6	23
β-strand	333	1	25
β-strand	336-337	2	26
α-helix	338	1
β-strand	345-346	2	26
α-helix	352-355	4
β-strand	358-362	5	23
α-helix	364-367	4
α-helix	368-381	14
β-strand	386	1	27
α-helix	388-399	12
α-helix	403-408	6
α-helix	410-419	10
β-strand	425	1	27
α-helix	427-436	10
β-strand	438	1	28
α-helix	440-447	8

Chain F: 22 helices, 26 β-strands

Element	Residues	Length	Sheet
β-strand	22	1	29
β-strand	33	1	30
β-strand	39	1	30
β-strand	42-43	2	31
β-strand	46-47	2	31
α-helix	50-65	16
β-strand	68	1	19
β-strand	72-77	6	28
α-helix	83-94	12
β-strand	100-104	5	28
α-helix	105-108	4
α-helix	115-125	11
β-strand	127-150	24	15
β-strand	158-164	7	15
β-strand	169-174	6	15
α-helix	175	1
α-helix	176-185	10
β-strand	191-196	6	15
β-strand	202-207	6	15
α-helix	210	1
β-strand	211	1	15
α-helix	212	1
α-helix	225-228	4
β-strand	233-243	11	15
α-helix	244-252	9
α-helix	257-262	6
α-helix	270-285	16
β-strand	289-293	5	15
β-strand	295-299	5	28
α-helix	301-303	3
β-strand	305	1	32
α-helix	306-315	10
β-strand	323-328	6	28
β-strand	332-334	3	33
α-helix	335	1
β-strand	336	1	32
β-strand	341-343	3	33
α-helix	348-351	4
β-strand	354-359	6	28
α-helix	364-378	15
β-strand	382	1	34
α-helix	384-396	13
α-helix	399-415	17
β-strand	421	1	34
α-helix	423-432	10
β-strand	434	1	35
α-helix	436-445	10
α-helix	447-449	3

Chain G: 25 helices, 26 β-strands

Element	Residues	Length	Sheet
β-strand	15	1	36
β-strand	26	1	37
α-helix	31	1
β-strand	32	1	37
α-helix	33	1
β-strand	35-36	2	38
β-strand	39-40	2	38
α-helix	43-58	16
β-strand	61	1	29
β-strand	65-69	5	35
α-helix	76-87	12
β-strand	93-97	5	35
α-helix	98-101	4
α-helix	108-118	11
β-strand	120-137	18	15
β-strand	140-143	4	15
β-strand	153-162	10	15
β-strand	167-172	6	15
α-helix	174-176	3
α-helix	177-182	6
β-strand	189-194	6	15
β-strand	200-206	7	15
α-helix	207-209	3
β-strand	214-215	2	39
β-strand	220-221	2	15
α-helix	222-225	4
β-strand	229-239	11	15
α-helix	240-248	9
α-helix	257-263	7
α-helix	273-289	17
β-strand	292-296	5	15
β-strand	298-302	5	35
α-helix	304-306	3
α-helix	309-319	11
α-helix	324-325	2
β-strand	326-331	6	35
β-strand	336-337	2	40
α-helix	338	1
β-strand	345-346	2	40
α-helix	352-355	4
β-strand	358-362	5	35
α-helix	365-367	3
α-helix	368-381	14
β-strand	386	1	41
α-helix	388-399	12
α-helix	403-408	6
α-helix	410-419	10
β-strand	425	1	41
α-helix	427-436	10
β-strand	438	1	42
α-helix	440-448	9

Chain H: 23 helices, 31 β-strands

Element	Residues	Length	Sheet
β-strand	22	1	43
β-strand	33	1	44
α-helix	38	1
β-strand	39	1	44
α-helix	40	1
β-strand	43	1	45
β-strand	46	1	45
α-helix	50-65	16
β-strand	68	1	36
β-strand	72-76	5	42
α-helix	83-93	11
β-strand	100-104	5	42
α-helix	105-108	4
α-helix	115-125	11
β-strand	127-133	7	46
β-strand	136-146	11	39
β-strand	160-164	5	39
β-strand	169-174	6	39
α-helix	176-184	9
β-strand	191-196	6	39
β-strand	201-207	7	39
α-helix	211-213	3
β-strand	217	1	47
β-strand	224	1	39
β-strand	225	1	7
α-helix	226-229	4
β-strand	233-235	3	39
β-strand	238-243	6	46
α-helix	244-250	7
α-helix	256-258	3
α-helix	259-262	4
α-helix	270-286	17
β-strand	289-293	5	46
β-strand	295-299	5	42
α-helix	301-303	3
β-strand	305	1	48
α-helix	306-315	10
α-helix	321-322	2
β-strand	323-328	6	42
β-strand	332-334	3	49
α-helix	335	1
β-strand	336	1	48
β-strand	341-343	3	49
α-helix	348-351	4
β-strand	354-358	5	42
α-helix	364-378	15
β-strand	382	1	50
α-helix	384-396	13
α-helix	399-415	17
β-strand	421	1	50
α-helix	423-432	10
β-strand	434	1	51
α-helix	436-445	10
β-strand	451	1	52

Chain I: 25 helices, 28 β-strands

Element	Residues	Length	Sheet
β-strand	15	1	53
β-strand	26	1	54
α-helix	31	1
β-strand	32	1	54
α-helix	33	1
β-strand	35-36	2	55
β-strand	39-40	2	55
α-helix	43-58	16
β-strand	61	1	43
β-strand	65-69	5	51
α-helix	76-87	12
β-strand	93-97	5	51
α-helix	98-101	4
α-helix	108-118	11
β-strand	120-140	21	47
β-strand	157-163	7	47
β-strand	166-172	7	47
α-helix	175-182	8
β-strand	189-194	6	47
β-strand	200-206	7	47
α-helix	207-209	3
β-strand	215	1	56
β-strand	220-221	2	47
α-helix	222-224	3
β-strand	229-239	11	47
α-helix	240-246	7
α-helix	256-263	8
α-helix	265-266	2
α-helix	273-289	17
β-strand	292-296	5	47
β-strand	298-302	5	51
α-helix	304-306	3
β-strand	308	1	57
α-helix	309-320	12
β-strand	326-331	6	51
β-strand	333	1	52
β-strand	336-337	2	58
α-helix	338	1
β-strand	339	1	57
β-strand	345-346	2	58
α-helix	347-349	3
α-helix	352-355	4
β-strand	358-362	5	51
α-helix	365-367	3
α-helix	368-382	15
β-strand	385-386	2	59
α-helix	388-400	13
α-helix	403-408	6
α-helix	410-419	10
β-strand	424-425	2	59
α-helix	427-436	10
β-strand	438	1	60
α-helix	440-448	9

4 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
E1A-binding protein p400,E1A-binding protein p400/Haloalkane dehalogenase chimera	A	protein	2841	Homo sapiens, Rhodococcus rhodochrous	Q96L91
Vacuolar protein sorting-associated protein 72 homolog	B	protein	364	Homo sapiens	Q15906 (AlphaFold model)
Enhancer of polycomb homolog 1	C	protein	263	Homo sapiens	Q9H2F5 (AlphaFold model)
RuvB-like 1	E, G, I	protein	456	Homo sapiens	Q9Y265 (AlphaFold model)
RuvB-like 2,RuvB-like 2/Maltose/maltodextrin-binding periplasmic protein chimera	F, H, J	protein	857	Homo sapiens, Escherichia coli K-12	Q9Y230
Actin, cytoplasmic 1	L	protein	375	Homo sapiens	P60709
Actin-like protein 6A	M	protein	429	Homo sapiens	O96019
DNA methyltransferase 1-associated protein 1	N	protein	467	Homo sapiens	Q9NPF5

Sequence of entity 1 (A), FASTA

>9CAE_1 E1A-binding protein p400,E1A-binding protein p400/Haloalkane dehalogenase chimera (chains A)
MALHVPTPGKVQVQASQLSSLPQMVASTRLPVDPAPPCPRPLPTSSTSSLAPVSGSGPGP
SPARSSPVNRPSSATNKALSPVTSRTPGVVASAPTKPQSPAQNATSSQDSSQDTLTEQIT
LENQVHQRIAELRKAGLWSQRRLPKLQEAPRPKSHWDYLLEEMQWMATDFAQERRWKVAA
AKKLVRTVVRHHEEKQLREERGKKEEQSRLRRIAASTAREIECFWSNIEQVVEIKLRVEL
EEKRKKALNLQKVSRRGKELRPKGFDALQESSLDSGMSGRKRKASISLTDDEVDDEEETI
EEEEANEGVVDHQTELSNLAKEAELPLLDLMKLYEGAFLPSSQWPRPKPDGEDTSGEEDA
DDCPGDRESRKDLVLIDSLFIMDQFKAAERMNIGKPNAKDIADVTAVAEAILPKGSARVT
TSVKFNAPSLLYGALRDYQKIGLDWLAKLYRKNLNGILADEAGLGKTVQIIAFFAHLACN
EGNWGPHLVVVRSCNILKWELELKRWCPGLKILSYIGSHRELKAKRQEWAEPNSFHVCIT
SYTQFFRGLTAFTRVRWKCLVIDEMQRVKGMTERHWEAVFTLQSQQRLLLIDSPLHNTFL
ELWTMVHFLVPGISRPYLSSPLRAPSEESQDYYHKVVIRLHRVTQPFILRRTKRDVEKQL
TKKYEHVLKCRLSNRQKALYEDVILQPGTQEALKSGHFVNVLSILVRLQRICNHPGLVEP
RHPGSSYVAGPLEYPSASLILKALERDFWKEADLSMFDLIGLENKITRHEAELLSKKKIP
RKLMEEISTSAAPAARPAAAKLKASRLFQPVQYGQKPEGRTVAFPSTHPPRTAAPTTASA
APQGPLRGRPPIATFSANPEAKAAAAPFQTSQASASAPRHQPASASSTAASPAHPAKLRA
QTTAQASTPGQPPPQPQAPSHAAGQSALPQRLVLPSQAQARLPSGEVVKIAQLASITGPQ
SRVAQPETPVTLQFQGSKFTLSHSQLRQLTAGQPLQLQGSVLQIVSAPGQPYLRAPGPVV
MQTVSQAGAVHGALGSKPPAGGPSPAPLTPQVGVPGRVAVNALAVGEPGTASKPASPIGG
PTQEEKTRLLKERLDQIYLVNERRCSQAPVYGRDLLRICALPSHGRVQWRGSLDGRRGKE
AGPAHSYTSSSESPSELMLTLCRCGESLQDVIDRVAFVIPPVVAAPPSLRVPRPPPLYSH
RMRILRQGLREHAAPYFQQLRQTTAPRLLQFPELRLVQFDSGKLEALAILLQKLKSEGRR
VLILSQMILMLDILEMFLNFHYLTYVRIDENASSEQRQELMRSFNRDRRIFCAILSTHSR
TTGINLVEADTVVFYDNDLNPVMDAKAQEWCDRIGRCKDIHIYRLVSGNSIEEKLLKNGT
KDLIREVAAQGNDYSMAFLTQRTIQELFEVYSPMDDAGFPVKAEEFVVLSQEPSVTETIA
PKIARPFIEALKSIEYLEEDAQKSAQEGVLGPHTDALSSDSENMPCDEEPSQLEELADFM
EQLTPIEKYALNYLELFHTSIEQEKERNSEDAVMTAVRAWEFWNLKTLQEREARLRLEQE
EAELLTYTREDAYSMEYVYEDVDGQTEVMPLWTPPTPPQDDSDIYLDSVMCLMYEATPIP
EAKLPPVYVRKERKRHKTDPSAAGRKKKQRHGEAVVPPRSLFDRATPGLLKIRREGKEQK
KNILLKQQVPFAKPLPTFAKPTAEPGQDNPEWLISEDWALLQAVKQLLELPLNLTIVSPA
HTPNWDLVSDVVNSCSRIYRSSKQCRNRYENVIIPREEGKSKNNRPLRTSQIYAQDENAT
HTQLYTSHFDLMKMTAGKRSPPIKPLLGMNPFQKNPKHASVLAESGINYDKPLPPIQVAS
LRAERIAKEKKALADQQKAQQPAVAQPPPPQPQPPPPPQQPPPPLPQPQAAGSQPPAGPP
AVQPQPQPQPQTQPQPVQAPAKAQPAITTGGSAAVLAGTIKTSVTGTSMPTGAVSGNVIV
NTIAGVPAATFQSINKRLASPVAPGALTTPGGSAPAQVVHTQPPPRAVGSPATATPDLVS
MATTQGVRAVTSVTASAVVTTNLTPVQTPARSLVPQVSQATGVQLPGKTITPAHFQLLRQ
QQQQQQQQQQQQQQQQQQQQQQQQQQQQTTTTSQVQVPQIQGQAQSPAQIKAVGKLTPEH
LIKMQKQKLQMPPQPPPPQAQSAPPQPAAQVQVQTSQPPQQQSPQLTTVTAPRPGALLTG
TTVANLQVARLTRVPTSQLQAQGQMQTQAPQPAQVALAKPPVVSVPAAVVSSPGVTTLPM
NVAGISVAIGQPQKAAGQTVVAQPVHMQQLLKLKQQAVQQQKAIQPQAAQGPAAVQQKIT
AQQITTPGAQQKVAYAAQPALKTQFLTTPISQAQKLAGAQQVQTQIQVAKLPQVVQQQTP
VASIQQVASASQQASPQTVALTQATAAGQQVQMIPAVTATAQVVQQKLIQQQVVTTASAP
LQTPGAPNPAQVPASSDSPSQQPKLQMRVPAVRLKTPTKPPCQGSGGSGEDLYFQSGGSM
AEIGTGFPFDPHYVEVLGERMHYVDVGPRDGTPVLFLHGNPTSSYVWRNIIPHVAPTHRC
IAPDLIGMGKSDKPDLGYFFDDHVRFMDAFIEALGLEEVVLVIHDWGSALGFHWAKRNPE
RVKGIAFMEFIRPIPTWDEWPEFARETFQAFRTTDVGRKLIIDQNVFIEGTLPMGVVRPL
TEVEMDHYREPFLNPVDREPLWRFPNELPIAGEPANIVALVEEYMDWLHQSPVPKLLFWG
TPGVLIPPAEAARLAKSLPNCKAVDIGPGLNLLQEDNPDLIGSEIARWLSTLEISGDYKD
HDGDYKDHDIDYKDDDDKGSG

Sequence of entity 2 (B), FASTA

>9CAE_2 Vacuolar protein sorting-associated protein 72 homolog (chains B)
MSLAGGRAPRKTAGNRLSGLLEAEEEDEFYQTTYGGFTEESGDDEYQGDQSDTEDEVDSD
FDIDEGDEPSSDGEAEEPRRKRRVVTKAYKEPLKSLRPRKVNTPAGSSQKAREEKALLPL
ELQDDGSDSRKSMRQSTAEHTRQTFLRVQERQGQSRRRKGPHCERPLTQEELLREAKITE
ELNLRSLETYERLEADKKKQVHKKRKCPGPIITYHSVTVPLVGEPGPKEENVDIEGLDPA
PSVSALTPHAGTGPVNPPARCSRTFITFSDDATFEEWFPQGRPPKVPVREVCPVTHRPAL
YRDPVTDIPYATARAFKIIREAYKKYITAHGLPPTASALGPGPPPPEPLPGSGPRALRQK
IVIK

Sequence of entity 3 (C), FASTA

>9CAE_3 Enhancer of polycomb homolog 1 (chains C)
MAALPVFNAKDLNQYDFPSSDEEPLSQVLSGSSEAEEDNDPDGPFAFRRKAGCQYYAPHL
DQTGNWPWTSPKDGGLGDVRYRYCLTTLTVPQRCIGFARRRVGRGGRVLLDRAHSDYDSV
FHHLDLEMLSSPQHSPVNQFANTSETNTSDKSFSKDLSQILVNIKSCRWRHFRPRTPSLH
DSDNDELSCRKLYRSINRTGTAQPGTQTCSTSTQSKSSSGSAHFAFTAEQYQQHQQQLAL
MQKQQLAQIQQQQANSNSSTNTS

Sequence of entity 4 (E, G, I), FASTA

>9CAE_4 RuvB-like 1 (chains E, G, I)
MKIEEVKSTTKTQRIASHSHVKGLGLDESGLAKQAASGLVGQENAREACGVIVELIKSKK
MAGRAVLLAGPPGTGKTALALAIAQELGSKVPFCPMVGSEVYSTEIKKTEVLMENFRRAI
GLRIKETKEVYEGEVTELTPCETENPMGGYGKTISHVIIGLKTAKGTKQLKLDPSIFESL
QKERVEAGDVIYIEANSGAVKRQGRCDTYATEFDLEAEEYVPLPKGDVHKKKEIIQDVTL
HDLDVANARPQGGQDILSMMGQLMKPKKTEITDKLRGEINKVVNKYIDQGIAELVPGVLF
VDEVHMLDIECFTYLHRALESSIAPIVIFASNRGNCVIRGTEDITSPHGIPLDLLDRVMI
IRTMLYTPQEMKQIIKIRAQTEGINISEEALNHLGEIGTKTTLRYSVQLLTPANLLAKIN
GKDSIEKEHVEEISELFYDAKSSAKILADQQDKYMK

Sequence of entity 5 (F, H, J), FASTA

>9CAE_5 RuvB-like 2,RuvB-like 2/Maltose/maltodextrin-binding periplasmic protein chimera (chains F, H, J)
MATVTATTKVPEIRDVTRIERIGAHSHIRGLGLDDALEPRQASQGMVGQLAARRAAGVVL
EMIREGKIAGRAVLIAGQPGTGKTAIAMGMAQALGPDTPFTAIAGSEIFSLEMSKTEALT
QAFRRSIGVRIKEETEIIEGEVVEIQIDRPATGTGSKVGKLTLKTTEMETIYDLGTKMIE
SLTKDKVQAGDVITIDKATGKISKLGRSFTRARDYDAMGSQTKFVQCPDGELQKRKEVVH
TVSLHEIDVINSRTQGFLALFSGDTGEIKSEVREQINAKVAEWREEGKAEIIPGVLFIDE
VHMLDIESFSFLNRALESDMAPVLIMATNRGITRIRGTSYQSPHGIPIDLLDRLLIVSTT
PYSEKDTKQILRIRCEEEDVEMSEDAYTVLTRIGLETSLRYAIQLITAASLVCRKRKGTE
VQVDDIKRVYSLFLDESRSTQYMKEYQDAFLFNELKGETMDTSGSGGSGLEVLFQGPGSS
GGASMKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGD
GPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSL
IYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGK
YDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNI
DTSKVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNK
DKPLGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQ
TVDEALKDAQTNGGSSG

Sequence of entity 6 (L), FASTA

>9CAE_6 Actin, cytoplasmic 1 (chains L)
MDDDIAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQS
KRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMT
QIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDL
AGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSY
ELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLS
GGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQ
EYDESGPSIVHRKCF

Sequence of entity 7 (M), FASTA

>9CAE_7 Actin-like protein 6A (chains M)
MSGGVYGGDEVGALVFDIGSYTVRAGYAGEDCPKVDFPTAIGMVVERDDGSTLMEIDGDK
GKQGGPTYYIDTNALRVPRENMEAISPLKNGMVEDWDSFQAILDHTYKMHVKSEASLHPV
LMSEAPWNTRAKREKLTELMFEHYNIPAFFLCKTAVLTAFANGRSTGLILDSGATHTTAI
PVHDGYVLQQGIVKSPLAGDFITMQCRELFQEMNIELVPPYMIASKEAVREGSPANWKRK
EKLPQVTRSWHNYMCNCVIQDFQASVLQVSDSTYDEQVAAQMPTVHYEFPNGYNCDFGAE
RLKIPEGLFDPSNVKGLSGNTMLGVSHVVTTSVGMCDIDIRPGLYGSVIVAGGNTLIQSF
TDRLNRELSQKTPPSMRLKLIANNTTVERRFSSWIGGSILASLGTFQQMWISKQEYEEGG
KQCVERKCP

Sequence of entity 8 (N), FASTA

>9CAE_8 DNA methyltransferase 1-associated protein 1 (chains N)
MATGADVRDILELGGPEGDAASGTISKKDIINPDKKKSKKSSETLTFKRPEGMHREVYAL
LYSDKKDAPPLLPSDTGQGYRTVKAKLGSKKVRPWKWMPFTNPARKDGAMFFHWRRAAEE
GKDYPFARFNKTVQVPVYSEQEYQLYLHDDAWTKAETDHLFDLSRRFDLRFVVIHDRYDH
QQFKKRSVEDLKERYYHICAKLANVRAVPGTDLKIPVFDAGHERRRKEQLERLYNRTPEQ
VAEEEYLLQELRKIEARKKEREKRSQDLQKLITAADTTAEQRRTERKAPKKKLPQKKEAE
KPAVPETAGIKFPDFKSAGVTLRSQRMKLPSSVGQKKIKALEQMLLELGVELSPTPTEEL
VHMFNELRSDLVLLYELKQACANCEYELQMLRHRHEALARAGVLGGPATPASGPGPASAE
PAVTEPGLGPDPKDTIIDVVGAPLTPNSRKRRESASSSSSVKKAKKP

Ligands and cofactors

ID	Name	Formula	Copies
AGS	Phosphothiophosphoric acid-adenylate ester	C10 H16 N5 O12 P3 S	8
MG	Magnesium ion	Mg	8

Primary citation

Structural divergence of H2A.Z-associated human chromatin remodelers SRCAP and TIP60. Park, G., Patel, A.B., Wu, C. et al. To be published.

Other PDB entries of the same protein (UniProt Q96L91), best resolution first:

9CAF 2.35 Å, Cryo-EM structure of the reconstituted TRRAP lobe of the human TIP60 complex (composite…
8QR1 2.4 Å, Cryo-EM structure of the human Tip60 complex
9C57 2.75 Å, Reconstituted P400 Subcomplex of the human TIP60 complex
9CAD 3.05 Å, Cryo-EM structure of the TRRAP lobe of the native human TIP60 complex (composite…
8XVT 3.2 Å, The core subcomplex of human NuA4/TIP60 complex
8XVV 3.2 Å, The TRRAP module of human NuA4/TIP60 complex
9C6N 3.29 Å, ARP module of the human TIP60 complex
9C47 3.4 Å, TRRAP module of the human TIP60 complex
9CAC 3.43 Å, Cryo-EM structure of the RuvBL lobe of the native human TIP60 complex (composite…
8QRI 3.5 Å, TRRAP and EP400 in the human Tip60 complex
9C62 5.28 Å, P400 subcomplex of the native human TIP60 complex
8XVG 9.4 Å, Structure of human NuA4/TIP60 complex

Browse structure collections

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