7D44: EIF2B-eIF2(aP), aP2 complex

eIF2B-eIF2(aP), aP2 complex. Determined by electron microscopy at 4.0 Å resolution. Released 9 Dec 2020.

Method: Electron microscopy
Resolution: 4.0 Å
Organism: Homo sapiens
Chains: 12
Atoms: 28,391
Mol. weight: 594.89 kDa
Released: 9 Dec 2020

Explore 7D44 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7D44 contains 157 α-helices and 194 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: 13 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	4-15	12
α-helix	22-35	14
α-helix	46-57	12
α-helix	63-76	14
α-helix	87-115	29
β-strand	123-126	4	1
α-helix	132-142	11
β-strand	148-153	6	1
α-helix	160-169	10
β-strand	175-178	4	1
α-helix	180-182	3
α-helix	183-186	4
β-strand	193-196	4	1
β-strand	206-209	4	2
α-helix	213-221	9
β-strand	226-229	4	1
α-helix	243-245	3
α-helix	248-251	4
β-strand	273-276	4	2
β-strand	283-286	4	1
β-strand	289-291	3	1
α-helix	293-303	11

Chain B: 12 helices, 12 β-strands

Element	Residues	Length	Sheet
α-helix	3-16	14
α-helix	22-34	13
α-helix	48-59	12
α-helix	63-76	14
α-helix	88-115	28
α-helix	116-118	3
β-strand	123-127	5	3
α-helix	132-143	12
β-strand	148-152	5	3
α-helix	161-169	9
β-strand	175-176	2	3
α-helix	186-189	4
β-strand	192-196	5	3
β-strand	200	1	4
β-strand	206	1	4
β-strand	207-209	3	5
α-helix	212-221	10
β-strand	226-229	4	3
β-strand	235	1	4
α-helix	248-251	4
β-strand	273-275	3	5
β-strand	283-286	4	3
β-strand	289-291	3	3
α-helix	293-304	12

Chain C: 18 helices, 13 β-strands

Element	Residues	Length	Sheet
α-helix	9-23	15
α-helix	31-47	17
α-helix	54-71	18
α-helix	77-95	19
α-helix	129-144	16
α-helix	147-155	9
β-strand	164-168	5	6
α-helix	172-181	10
β-strand	188-193	6	6
α-helix	199-206	8
α-helix	207-210	4
β-strand	214-218	5	6
α-helix	219-221	3
α-helix	222-226	5
β-strand	231-234	4	6
β-strand	238-239	2	7
β-strand	245-248	4	7
α-helix	252-260	9
β-strand	265-268	4	6
α-helix	271-273	3
β-strand	274	1	7
β-strand	288	1	8
α-helix	297-299	3
α-helix	301-304	4
β-strand	311	1	8
β-strand	313-315	3	7
α-helix	318-320	3
β-strand	323-326	4	6
β-strand	329-331	3	6
α-helix	335-342	8
α-helix	346-350	5

Chain D: 18 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	9-24	16
α-helix	31-47	17
α-helix	54-71	18
α-helix	76-95	20
α-helix	128-145	18
α-helix	147-155	9
α-helix	156-158	3
β-strand	164-165	2	9
β-strand	168	1	9
α-helix	172-180	9
β-strand	188-193	6	9
α-helix	200-208	9
β-strand	214-218	5	9
α-helix	222-225	4
α-helix	226-228	3
β-strand	231-234	4	9
β-strand	238	1	10
β-strand	239	1	11
β-strand	246-248	3	10
α-helix	251-260	10
β-strand	265-267	3	9
α-helix	271-273	3
β-strand	274	1	11
α-helix	279-281	3
β-strand	288	1	12
α-helix	291-293	3
α-helix	301-304	4
β-strand	306	1	13
β-strand	311	1	12
β-strand	313-315	3	10
β-strand	323-327	5	9
β-strand	329-331	3	9
α-helix	339-343	5
α-helix	346-348	3

Chain E: 10 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	14
α-helix	37-43	7
β-strand	51-55	5	14
α-helix	63-66	4
β-strand	78-79	2	14
α-helix	86-93	8
α-helix	94-96	3
β-strand	100-103	4	14
β-strand	109	1	15
α-helix	114-123	10
β-strand	129-133	5	16
β-strand	156-161	6	17
β-strand	166	1	16
β-strand	167-172	6	17
β-strand	193-196	4	17
β-strand	200-201	2	16
α-helix	210-216	7
α-helix	224-228	5
α-helix	229-235	7
β-strand	264-267	4	16
β-strand	272	1	15
α-helix	278-291	14
α-helix	292-294	3
β-strand	350	1	18
β-strand	356	1	19
β-strand	366	1	18
β-strand	373	1	19
β-strand	385	1	20
β-strand	391-392	2	21
β-strand	402-403	2	20
β-strand	408-409	2	21
β-strand	419-420	2	20
β-strand	425	1	21

Chain F: 9 helices, 18 β-strands

Element	Residues	Length	Sheet
α-helix	37-45	9
β-strand	52-54	3	22
α-helix	63-67	5
β-strand	76-78	3	22
α-helix	86-93	8
β-strand	101-103	3	23
α-helix	114-122	9
β-strand	128-133	6	23
β-strand	157-160	4	24
β-strand	169-171	3	24
α-helix	184-189	6
β-strand	192-196	5	24
β-strand	205-207	3	23
α-helix	209-217	9
α-helix	224-228	5
α-helix	229-235	7
β-strand	263-268	6	23
α-helix	279-291	13
β-strand	374	1	25
β-strand	380-381	2	26
β-strand	385	1	27
β-strand	391	1	25
β-strand	397-398	2	26
β-strand	402	1	27
β-strand	403	1	28
β-strand	420	1	28
β-strand	436	1	28

Chain G: 16 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	178-180	3
β-strand	185	1	29
α-helix	192-194	3
α-helix	205-215	11
α-helix	222-237	16
α-helix	248-266	19
α-helix	271-286	16
α-helix	293-308	16
α-helix	309-313	5
α-helix	314-323	10
β-strand	333-334	2	30
α-helix	340-351	12
β-strand	358-359	2	30
β-strand	360-362	3	31
α-helix	369-377	9
β-strand	385-387	3	31
α-helix	388-393	6
β-strand	403	1	32
β-strand	408	1	33
β-strand	414-417	4	34
α-helix	418-430	13
β-strand	436-437	2	32
β-strand	443	1	33
β-strand	457	1	29
α-helix	460-462	3
β-strand	482-484	3	6
β-strand	489-492	4	34
β-strand	500-502	3	32
β-strand	505-507	3	32
α-helix	509-511	3
α-helix	512-515	4

Chain H: 20 helices, 18 β-strands

Element	Residues	Length	Sheet
α-helix	170-172	3
α-helix	178-180	3
α-helix	192-195	4
α-helix	205-215	11
α-helix	222-237	16
α-helix	242-243	2
α-helix	248-266	19
α-helix	271-286	16
α-helix	293-308	16
α-helix	309-313	5
α-helix	314-323	10
α-helix	324-326	3
β-strand	334	1	35
α-helix	340-349	10
β-strand	358	1	13
β-strand	359	1	35
β-strand	361-362	2	36
α-helix	370-377	8
β-strand	383	1	13
β-strand	386-387	2	36
α-helix	388-390	3
α-helix	391-394	4
β-strand	401-404	4	35
β-strand	407	1	37
β-strand	414-416	3	37
α-helix	420-429	10
β-strand	434-437	4	35
β-strand	457	1	38
α-helix	460-462	3
β-strand	467	1	39
β-strand	470	1	39
β-strand	482-484	3	9
β-strand	487	1	38
β-strand	490-492	3	37
β-strand	500-502	3	35
β-strand	505-507	3	35
α-helix	509-511	3
α-helix	513-516	4

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
Translation initiation factor eIF-2B subunit alpha	A, B	protein	305	Homo sapiens	Q14232 (AlphaFold model)
Translation initiation factor eIF-2B subunit beta	C, D	protein	351	Homo sapiens	P49770 (AlphaFold model)
Translation initiation factor eIF-2B subunit gamma	E, F	protein	452	Homo sapiens	Q9NR50 (AlphaFold model)
Translation initiation factor eIF-2B subunit delta	G, H	protein	523	Homo sapiens	Q9UI10 (AlphaFold model)
Translation initiation factor eIF-2B subunit epsilon	I, J	protein	721	Homo sapiens	Q13144
Eukaryotic translation initiation factor 2 subunit 1	K, L	protein	315	Homo sapiens	P05198

Sequence of entity 1 (A, B), FASTA

>7D44_1 Translation initiation factor eIF-2B subunit alpha (chains A, B)
MDDKELIEYFKSQMKEDPDMASAVAAIRTLLEFLKRDKGETIQGLRANLTSAIETLCGVD
SSVAVSSGGELFLRFISLASLEYSDYSKCKKIMIERGELFLRRISLSRNKIADLCHTFIK
DGATILTHAYSRVVLRVLEAAVAAKKRFSVYVTESQPDLSGKKMAKALCHLNVPVTVVLD
AAVGYIMEKADLVIVGAEGVVENGGIINKIGTNQMAVCAKAQNKPFYVVAESFKFVRLFP
LNQQDVPDKFKYKADTLKVAQTGQDLKEEHPWVDYTAPSLITLLFTDLGVLTPSAVSDEL
IKLYL

Sequence of entity 2 (C, D), FASTA

>7D44_2 Translation initiation factor eIF-2B subunit beta (chains C, D)
MPGSAAKGSELSERIESFVETLKRGGGPRSSEEMARETLGLLRQIITDHRWSNAGELMEL
IRREGRRMTAAQPSETTVGNMVRRVLKIIREEYGRLHGRSDESDQQESLHKLLTSGGLNE
DFSFHYAQLQSNIIEAINELLVELEGTMENIAAQALEHIHSNEVIMTIGFSRTVEAFLKE
AARKRKFHVIVAECAPFCQGHEMAVNLSKAGIETTVMTDAAIFAVMSRVNKVIIGTKTIL
ANGALRAVTGTHTLALAAKHHSTPLIVCAPMFKLSPQFPNEEDSFHKFVAPEEVLPFTEG
DILEKVSVHCPVFDYVPPELITLFISNIGGNAPSYIYRLMSELYHPDDHVL

Sequence of entity 3 (E, F), FASTA

>7D44_3 Translation initiation factor eIF-2B subunit gamma (chains E, F)
MEFQAVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTTRDVQ
KALCAEFKMKMKPDIVCIPDDADMGTADSLRYIYPKLKTDVLVLSCDLITDVALHEVVDL
FRAYDASLAMLMRKGQDSIEPVPGQKGKKKAVEQRDFIGVDSTGKRLLFMANEADLDEEL
VIKGSILQKHPRIRFHTGLVDAHLYCLKKYIVDFLMENGSITSIRSELIPYLVRKQFSSA
SSQQGQEEKEEDLKKKELKSLDIYSFIKEANTLNLAPYDACWNACRGDRWEDLSRSQVRC
YVHIMKEGLCSRVSTLGLYMEANRQVPKLLSALCPEEPPVHSSAQIVSKHLVGVDSLIGP
ETQIGEKSSIKRSVIGSSCLIKDRVTITNCLLMNSVTVEEGSNIQGSVICNNAVIEKGAD
IKDCLIGSGQRIEAKAKRVNEVIVGNDQLMEI

Sequence of entity 4 (G, H), FASTA

>7D44_4 Translation initiation factor eIF-2B subunit delta (chains G, H)
MAAVAVAVREDSGSGMKAELPPGPGAVGREMTKEEKLQLRKEKKQQKKKRKEEKGAEPET
GSAVSAAQCQVGPTRELPESGIQLGTPREKVPAGRSKAELRAERRAKQEAERALKQARKG
EQGGPPPKASPSTAGETPSGVKRLPEYPQVDDLLLRRLVKKPERQQVPTRKDYGSKVSLF
SHLPQYSRQNSLTQFMSIPSSVIHPAMVRLGLQYSQGLVSGSNARCIALLRALQQVIQDY
TTPPNEELSRDLVNKLKPYMSFLTQCRPLSASMHNAIKFLNKEITSVGSSKREEEAKSEL
RAAIDRYVQEKIVLAAQAISRFAYQKISNGDVILVYGCSSLVSRILQEAWTEGRRFRVVV
VDSRPWLEGRHTLRSLVHAGVPASYLLIPAASYVLPEVSKVLLGAHALLANGSVMSRVGT
AQLALVARAHNVPVLVCCETYKFCERVQTDAFVSNELDDPDDLQCKRGEHVALANWQNHA
SLRLLNLVYDVTPPELVDLVITELGMIPCSSVPVVLRVKSSDQ

Sequence of entity 5 (I, J), FASTA

>7D44_5 Translation initiation factor eIF-2B subunit epsilon (chains I, J)
MAAPVVAPPGVVVSRANKRSGAGPGGSGGGGARGAEEEPPPPLQAVLVADSFDRRFFPIS
KDQPRVLLPLANVALIDYTLEFLTATGVQETFVFCCWKAAQIKEHLLKSKWCRPTSLNVV
RIITSELYRSLGDVLRDVDAKALVRSDFLLVYGDVISNINITRALEEHRLRRKLEKNVSV
MTMIFKESSPSHPTRCHEDNVVVAVDSTTNRVLHFQKTQGLRRFAFPLSLFQGSSDGVEV
RYDLLDCHISICSPQVAQLFTDNFDYQTRDDFVRGLLVNEEILGNQIHMHVTAKEYGARV
SNLHMYSAVCADVIRRWVYPLTPEANFTDSTTQSCTHSRHNIYRGPEVSLGHGSILEENV
LLGSGTVIGSNCFITNSVIGPGCHIGDNVVLDQTYLWQGVRVAAGAQIHQSLLCDNAEVK
ERVTLKPRSVLTSQVVVGPNITLPEGSVISLHPPDAEEDEDDGEFSDDSGADQEKDKVKM
KGYNPAEVGAAGKGYLWKAAGMNMEEEEELQQNLWGLKINMEEESESESEQSMDSEEPDS
RGGSPQMDDIKVFQNEVLGTLQRGKEENISCDNLVLEINSLKYAYNISLKEVMQVLSHVV
LEFPLQQMDSPLDSSRYCALLLPLLKAWSPVFRNYIKRAADHLEALAAIEDFFLEHEALG
ISMAKVLMAFYQLEILAEETILSWFSQRDTTDKGQQLRKNQQLQRFIQWLKEAEEESSED
D

Sequence of entity 6 (K, L), FASTA

>7D44_6 Eukaryotic translation initiation factor 2 subunit 1 (chains K, L)
MPGLSCRFYQHKFPEVEDVVMVNVRSIAEMGAYVSLLEYNNIEGMILLSELSRRRIRSIN
KLIRIGRNECVVVIRVDKEKGYIDLSKRRVSPEEAIKCEDKFTKSKTVYSILRHVAEVLE
YTKDEQLESLFQRTAWVFDDKYKRPGYGAYDAFKHAVSDPSILDSLDLNEDEREVLINNI
NRRLTPQAVKIRADIEVACYGYEGIDAVKEALRAGLNCSTENMPIKINLIAPPRYVMTTT
TLERTEGLSVLSQAMAVIKEKIEEKRGVFNVQMEPKVVTDTDETELARQMERLERENAEV
DGDDDAEEMEAKAED

Primary citation

ISRIB Blunts the Integrated Stress Response by Allosterically Antagonising the Inhibitory Effect of Phosphorylated eIF2 on eIF2B. Zyryanova, A.F., Kashiwagi, K., Rato, C. et al. Mol Cell (2021) 81:88. DOI 10.1016/j.molcel.2020.10.031 · PubMed

Other PDB entries of the same protein (UniProt Q14232 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9Y4B 2.1 Å, Eukaryotic translation initiation factor 2-B (eIF2B) with a truncation in the beta…
9ZUZ 2.25 Å, Translation Initiation Factor eIF-2B complex with the Isohexide Diamine GSK735
7VLK 2.27 Å, eIF2B-SFSV NSs C2-imposed
9Y3U 2.4 Å, Eukaryotic translation initiation factor 2-B (eIF2B) with a truncation in the beta…
9Y4W 2.4 Å, Eukaryotic translation initiation factor 2-B (eIF2B) with a truncation in the beta…
7F64 2.42 Å, eIF2B-SFSV NSs
9Y3T 2.5 Å, Eukaryotic translation initiation factor 2-B (eIF2B) with a truncation in the beta…
7RLO 2.6 Å, Structure of the human eukaryotic translation initiation factor 2B (eIF2B) in complex…
3ECS 2.65 Å, Crystal structure of human eIF2B alpha
7KMA 2.7 Å, Crystal structure of eif2Balpha with a ligand.
9HVE 2.7 Å, Native human eIF2-eIF2B complex
7F66 2.76 Å, eIF2B-SFSV NSs-1-eIF2

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