Research workbench

EIF2B-EIF2(AP), apg complex

Analyse EIF2B-EIF2(AP), apg complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7D43
Type: protein
Length: 4,347 residues
Chains: 14
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Translation initiation factor eif-2B subunit alpha; Translation initiation factor eif-2B…
EC: 3.6.5.3
UniProt: Q14232, P49770, Q9NR50, Q9UI10, Q13144, P05198, P20042, P41091
Pockets: 20 · best druggability 0.87

Structure

electron microscopy · 13 distinct chains · 31% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Translation initiation factor eif-2B subunit alpha	protein	293	47% helix, 11% strand	Q14232
B	Translation initiation factor eif-2B subunit alpha	protein	291	46% helix, 9% strand	Q14232
C	Translation initiation factor eif-2B subunit beta	protein	317	50% helix, 10% strand	P49770
D	Translation initiation factor eif-2B subunit beta	protein	324	50% helix, 10% strand	P49770
E	Translation initiation factor eif-2B subunit gamma	protein	344	19% helix, 14% strand	Q9NR50
F	Translation initiation factor eif-2B subunit gamma	protein	343	20% helix, 13% strand	Q9NR50
G, H	Translation initiation factor eif-2B subunit delta	protein	353	44% helix, 12% strand	Q9UI10
I	Translation initiation factor eif-2B subunit epsilon	protein	427	19% helix, 16% strand	Q13144
J	Translation initiation factor eif-2B subunit epsilon	protein	429	20% helix, 16% strand	Q13144
K	Eukaryotic translation initiation factor 2 subunit 1	protein	260	41% helix, 13% strand	P05198
L	Eukaryotic translation initiation factor 2 subunit 1	protein	176	39% helix, 14% strand	P05198
M	Eukaryotic translation initiation factor 2 subunit 2	protein	16	44% helix, 0% strand	P20042
P	Eukaryotic translation initiation factor 2 subunit 3 (EC 3.6.5.3)	protein	421	3% helix, 7% strand	P41091

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	988	0.87	0.88	122	empty
2	1034	0.87	0.88	113	empty
3	1001	0.83	0.84	175	empty
4	675	0.82	0.87	73	empty
5	572	0.79	0.86	66	empty

Interfaces

29 interfaces between chains.

D–H · 2297 Å² buried · 22 hydrogen bonds · protein-protein
C–G · 2285 Å² buried · 19 hydrogen bonds · protein-protein
C–I · 1380 Å² buried · 9 hydrogen bonds · protein-protein
A–B · 1304 Å² buried · 11 hydrogen bonds · protein-protein
D–J · 1299 Å² buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (phosphorylation).

Compared structures

7D43 · eIF2B-eIF2(aP), aPg complex · the same entry in another collection · chain K against K, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q14232
Every structure of UniProt P49770
Every structure of UniProt Q9NR50
Every structure of UniProt Q9UI10
Every structure of UniProt Q13144
Every structure of UniProt P05198
Every structure of UniProt P20042
Every structure of UniProt P41091
Elsewhere: RCSB PDB 7D43 · PDBe 7D43 · UniProt Q14232 · UniProt P49770 · UniProt Q9NR50 · UniProt Q9UI10 · UniProt Q13144 · UniProt P05198 · UniProt P20042 · UniProt P41091

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