7L7G: PDB entry 7L7G

Name: PDB 7L7G: Electron cryo-microscopy of the eukaryotic translation initiation factor 2B from Homo sapiens (updated model of PDB ID: 6CAJ)
Published: 2021-03-24
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: translation

Electron cryo-microscopy of the eukaryotic translation initiation factor 2B from Homo sapiens (updated model of PDB ID: 6CAJ). Determined by electron microscopy at 3.0 Å resolution. Released 24 Mar 2021.

Method: Electron microscopy
Resolution: 3.0 Å
Organism: Homo sapiens
Chains: 10
Atoms: 25,086
Mol. weight: 526.77 kDa
Ligands: C7B
Released: 24 Mar 2021

Explore 7L7G in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7L7G contains 155 α-helices and 176 β-strands across 10 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.

Chains A and B: 13 helices, 35 β-strands

Element	Residues	Length	Sheet
β-strand	44-48	5	16
α-helix	59-62	4
α-helix	65-67	3
β-strand	69	1	17
β-strand	74	1	17
α-helix	75-86	12
β-strand	90-95	6	16
α-helix	99-107	9
α-helix	110-112	3
β-strand	119-124	6	16
α-helix	131-141	11
β-strand	148-152	5	16
β-strand	155-157	3	18
α-helix	162-174	13
β-strand	179-187	9	16
β-strand	201-206	6	16
β-strand	211-217	7	16
β-strand	223	1	19
α-helix	230-233	4
β-strand	238-241	4	16
β-strand	244-246	3	16
β-strand	251-252	2	16
α-helix	254-262	9
α-helix	269-277	9
β-strand	286-292	7	16
β-strand	297-299	3	18
α-helix	303-314	12
β-strand	336-338	3	20
α-helix	339-341	3
β-strand	342-344	3	20
β-strand	355-356	2	21
β-strand	360-362	3	20
β-strand	367-368	2	22
β-strand	373-375	3	21
β-strand	378-379	2	20
β-strand	384-385	2	22
β-strand	390-392	3	21
β-strand	395-396	2	20
β-strand	401-402	2	22
β-strand	407-409	3	21
β-strand	411-413	3	23
β-strand	418-419	2	22
β-strand	423-425	3	21
β-strand	429-431	3	23
β-strand	436-437	2	22
β-strand	441-443	3	21
β-strand	447-449	3	23
α-helix	453-455	3

Chains C and D: 19 helices, 14 β-strands

Element	Residues	Length	Sheet
α-helix	9-24	16
α-helix	31-47	17
α-helix	54-71	18
α-helix	76-97	22
α-helix	127-144	18
α-helix	146-154	9
α-helix	155-158	4
β-strand	163-168	6	10
α-helix	172-181	10
β-strand	187-192	6	10
α-helix	193-194	2
α-helix	199-209	11
β-strand	214-217	4	10
α-helix	219-221	3
α-helix	222-226	5
β-strand	231-234	4	10
β-strand	238-239	2	11
β-strand	245-248	4	11
α-helix	251-261	11
β-strand	265-268	4	10
β-strand	274	1	11
β-strand	288	1	12
α-helix	291-293	3
α-helix	297-304	8
β-strand	306-308	3	13
β-strand	311	1	12
β-strand	313-316	4	11
α-helix	318-320	3
β-strand	323-325	3	10
β-strand	330-331	2	10
α-helix	333-335	3
α-helix	336-343	8
α-helix	346-348	3

Chain E: 23 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	167-171	5
α-helix	178-180	3
β-strand	185	1	29
α-helix	193-195	3
α-helix	205-215	11
α-helix	222-239	18
α-helix	242-243	2
α-helix	248-266	19
α-helix	268-270	3
α-helix	271-285	15
α-helix	294-308	15
α-helix	309-314	6
α-helix	315-324	10
β-strand	332-336	5	28
α-helix	340-352	13
β-strand	357-362	6	28
α-helix	369-379	11
β-strand	383-387	5	28
α-helix	388-390	3
α-helix	391-394	4
β-strand	400-404	5	28
β-strand	407-408	2	30
β-strand	414-417	4	30
α-helix	420-429	10
β-strand	434-437	4	28
α-helix	440-442	3
β-strand	443	1	30
β-strand	457	1	29
α-helix	460-463	4
α-helix	476-478	3
β-strand	482-484	3	25
β-strand	487	1	29
β-strand	489-492	4	30
α-helix	494-496	3
β-strand	499-502	4	28
β-strand	505-507	3	28
α-helix	509-511	3
α-helix	512-518	7

Chain F: 22 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	167-171	5
α-helix	178-180	3
β-strand	185	1	14
α-helix	193-195	3
α-helix	205-215	11
α-helix	222-239	18
α-helix	242-243	2
α-helix	248-266	19
α-helix	268-270	3
α-helix	271-285	15
α-helix	294-308	15
α-helix	309-314	6
α-helix	315-324	10
β-strand	332-336	5	13
α-helix	340-352	13
β-strand	357-362	6	13
α-helix	369-379	11
β-strand	383-387	5	13
α-helix	388-390	3
α-helix	391-394	4
β-strand	400-404	5	13
β-strand	407-408	2	15
β-strand	414-417	4	15
α-helix	420-429	10
β-strand	434-437	4	13
α-helix	440-442	3
β-strand	443	1	15
β-strand	457	1	14
α-helix	460-463	4
β-strand	482-484	3	10
β-strand	487	1	14
β-strand	489-492	4	15
α-helix	494-496	3
β-strand	499-502	4	13
β-strand	505-507	3	13
α-helix	509-511	3
α-helix	512-518	7

Chains G and H: 16 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	6-16	11
α-helix	22-37	16
α-helix	46-59	14
α-helix	63-77	15
α-helix	87-115	29
α-helix	116-118	3
β-strand	124-127	4	33
α-helix	132-143	12
β-strand	149-153	5	33
α-helix	160-169	10
β-strand	175-178	4	33
α-helix	183-186	4
α-helix	187-189	3
β-strand	192-196	5	33
β-strand	200	1	34
β-strand	206-209	4	34
α-helix	212-221	10
β-strand	226-229	4	33
α-helix	232-234	3
β-strand	235	1	34
α-helix	243-245	3
α-helix	248-251	4
β-strand	273-276	4	34
α-helix	278-280	3
β-strand	283-286	4	33
β-strand	289-291	3	33
α-helix	295-303	9

Chain I: 7 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	3-8	6	24
α-helix	37-45	9
β-strand	52-54	3	24
β-strand	76-78	3	24
α-helix	87-93	7
α-helix	94-96	3
β-strand	100-105	6	24
α-helix	115-123	9
β-strand	128-133	6	24
β-strand	156-160	5	16
β-strand	166	1	24
β-strand	167-172	6	16
β-strand	183	1	19
α-helix	184-189	6
β-strand	192-196	5	16
β-strand	200-201	2	24
β-strand	205-207	3	24
α-helix	209-217	9
α-helix	224-227	4
β-strand	300-304	5	24

Chain J: 7 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	3-8	6	9
α-helix	37-45	9
β-strand	52-54	3	9
β-strand	76-78	3	9
α-helix	87-93	7
α-helix	94-96	3
β-strand	100-105	6	9
α-helix	115-123	9
β-strand	128-133	6	9
β-strand	156-160	5	1
β-strand	166	1	9
β-strand	167-172	6	1
β-strand	183	1	4
α-helix	184-189	6
β-strand	193-196	4	1
β-strand	200-201	2	9
β-strand	205-207	3	9
α-helix	209-217	9
α-helix	224-227	4
β-strand	300-304	5	9

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Translation initiation factor eIF-2B subunit epsilon	A, B	protein	721	Homo sapiens	Q13144 (AlphaFold model)
Translation initiation factor eIF-2B subunit gamma	I, J	protein	452	Homo sapiens	Q9NR50 (AlphaFold model)
Translation initiation factor eIF-2B subunit beta	C, D	protein	368	Homo sapiens	P49770 (AlphaFold model)
Translation initiation factor eIF-2B subunit delta	E, F	protein	523	Homo sapiens	Q9UI10 (AlphaFold model)
Translation initiation factor eIF-2B subunit alpha	G, H	protein	305	Homo sapiens	Q14232

Sequence of entity 1 (A, B), FASTA

>7L7G_1 Translation initiation factor eIF-2B subunit epsilon (chains A, B)
MAAPVVAPPGVVVSRANKRSGAGPGGSGGGGARGAEEEPPPPLQAVLVADSFDRRFFPIS
KDQPRVLLPLANVALIDYTLEFLTATGVQETFVFCCWKAAQIKEHLLKSKWCRPTSLNVV
RIITSELYRSLGDVLRDVDAKALVRSDFLLVYGDVISNINITRALEEHRLRRKLEKNVSV
MTMIFKESSPSHPTRCHEDNVVVAVDSTTNRVLHFQKTQGLRRFAFPLSLFQGSSDGVEV
RYDLLDCHISICSPQVAQLFTDNFDYQTRDDFVRGLLVNEEILGNQIHMHVTAKEYGARV
SNLHMYSAVCADVIRRWVYPLTPEANFTDSTTQSCTHSRHNIYRGPEVSLGHGSILEENV
LLGSGTVIGSNCFITNSVIGPGCHIGDNVVLDQTYLWQGVRVAAGAQIHQSLLCDNAEVK
ERVTLKPRSVLTSQVVVGPNITLPEGSVISLHPPDAEEDEDDGEFSDDSGADQEKDKVKM
KGYNPAEVGAAGKGYLWKAAGMNMEEEEELQQNLWGLKINMEEESESESEQSMDSEEPDS
RGGSPQMDDIKVFQNEVLGTLQRGKEENISCDNLVLEINSLKYAYNVSLKEVMQVLSHVV
LEFPLQQMDSPLDSSRYCALLLPLLKAWSPVFRNYIKRAADHLEALAAIEDFFLEHEALG
ISMAKVLMAFYQLEILAEETILSWFSQRDTTDKGQQLRKNQQLQRFIQWLKEAEEESSED
D

Sequence of entity 2 (I, J), FASTA

>7L7G_2 Translation initiation factor eIF-2B subunit gamma (chains I, J)
MEFQAVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTTRDVQ
KALCAEFKMKMKPDIVCIPDDADMGTADSLRYIYPKLKTDVLVLSCDLITDVALHEVVDL
FRAYDASLAMLMRKGQDSIEPVPGQKGKKKAVEQRDFIGVDSTGKRLLFMANEADLDEEL
VIKGSILQKHPRIRFHTGLVDAHLYCLKKYIVDFLMENGSITSIRSELIPYLVRKQFSSA
SSQQGQEEKEEDLKKKELKSLDIYSFIKEANTLNLAPYDACWNACRGDRWEDLSRSQVRC
YVHIMKEGLCSRVSTLGLYMEANRQVPKLLSALCPEEPPVHSSAQIVSKHLVGVDSLIGP
ETQIGEKSSIKRSVIGSSCLIKDRVTITNCLLMNSVTVEEGSNIQGSVICNNAVIEKGAD
IKDCLIGSGQRIEAKAKRVNEVIVGNDQLMEI

Sequence of entity 3 (C, D), FASTA

>7L7G_3 Translation initiation factor eIF-2B subunit beta (chains C, D)
MHHHHHHGGGSENLYFQSPGSAAKGSELSERIESFVETLKRGGGPRSSEEMARETLGLLR
QIITDHRWSNAGELMELIRREGRRMTAAQPSETTVGNMVRRVLKIIREEYGRLHGRSDES
DQQESLHKLLTSGGLNEDFSFHYAQLQSNIIEAINELLVELEGTMENIAAQALEHIHSNE
VIMTIGFSRTVEAFLKEAARKRKFHVIVAECAPFCQGHEMAVNLSKAGIETTVMTDAAIF
AVMSRVNKVIIGTKTILANGALRAVTGTHTLALAAKHHSTPLIVCAPMFKLSPQFPNEED
SFHKFVAPEEVLPFTEGDILEKVSVHCPVFDYVPPELITLFISNIGGNAPSYIYRLMSEL
YHPDDHVL

Sequence of entity 4 (E, F), FASTA

>7L7G_4 Translation initiation factor eIF-2B subunit delta (chains E, F)
MAAVAVAVREDSGSGMKAELPPGPGAVGREMTKEEKLQLRKEKKQQKKKRKEEKGAEPET
GSAVSAAQCQVGPTRELPESGIQLGTPREKVPAGRSKAELRAERRAKQEAERALKQARKG
EQGGPPPKASPSTAGETPSGVKRLPEYPQVDDLLLRRLVKKPERQQVPTRKDYGSKVSLF
SHLPQYSRQNSLTQFMSIPSSVIHPAMVRLGLQYSQGLVSGSNARCIALLRALQQVIQDY
TTPPNEELSRDLVNKLKPYMSFLTQCRPLSASMHNAIKFLNKEITSVGSSKREEEAKSEL
RAAIDRYVQEKIVLAAQAISRFAYQKISNGDVILVYGCSSLVSRILQEAWTEGRRFRVVV
VDSRPWLEGRHTLRSLVHAGVPASYLLIPAASYVLPEVSKVLLGAHALLANGSVMSRVGT
AQLALVARAHNVPVLVCCETYKFCERVQTDAFVSNELDDPDDLQCKRGEHVALANWQNHA
SLRLLNLVYDVTPPELVDLVITELGMIPCSSVPVVLRVKSSDQ

Sequence of entity 5 (G, H), FASTA

>7L7G_5 Translation initiation factor eIF-2B subunit alpha (chains G, H)
MDDKELIEYFKSQMKEDPDMASAVAAIRTLLEFLKRDKGETIQGLRANLTSAIETLCGVD
SSVAVSSGGELFLRFISLASLEYSDYSKCKKIMIERGELFLRRISLSRNKIADLCHTFIK
DGATILTHAYSRVVLRVLEAAVAAKKRFSVYVTESQPDLSGKKMAKALCHLNVPVTVVLD
AAVGYIMEKADLVIVGAEGVVENGGIINKIGTNQMAVCAKAQNKPFYVVAESFKFVRLFP
LNQQDVPDKFKYKADTLKVAQTGQDLKEEHPWVDYTAPSLITLLFTDLGVLTPSAVSDEL
IKLYL

Ligands and cofactors

ID	Name	Formula	Copies
C7B	2-(4-chloranylphenoxy)-~{N}-[4-[2-(4-chloranylphenoxy)ethanoylamino]cyclohexyl]…	C22 H24 Cl2 N2 O4	1

Primary citation

eIF2B conformation and assembly state regulates the integrated stress response. Schoof, M., Boone, M., Wang, L. et al. Elife (2021) 10. DOI 10.7554/eLife.65703 · PubMed

Other PDB entries of the same protein (UniProt Q13144 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3JUI 2.0 Å, Crystal Structure of the C-terminal Domain of Human Translation Initiation Factor eIF2B…
9Y4B 2.1 Å, Eukaryotic translation initiation factor 2-B (eIF2B) with a truncation in the beta…
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…
9HVE 2.7 Å, Native human eIF2-eIF2B complex
7F66 2.76 Å, eIF2B-SFSV NSs-1-eIF2
9Y5T 2.78 Å, eIF2B lacking the latch helix bound to ISRACT-02 (Active state)
6CAJ 2.8 Å, Electron cryo-microscopy of the eukaryotic translation initiation factor 2B from Homo…

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