Research workbench

EIF2B-EIF2(AP), AP1 complex

Analyse EIF2B-EIF2(AP), AP1 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7D45
Type: protein
Length: 3,659 residues
Chains: 11
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Translation initiation factor eif-2B subunit alpha; Translation initiation factor eif-2B…
UniProt: Q14232, P49770, Q9NR50, Q9UI10, Q13144, P05198
Pockets: 20 · best druggability 0.86

Structure

electron microscopy · 10 distinct chains · 33% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Translation initiation factor eif-2B subunit alpha	protein	293	45% helix, 12% strand	Q14232
B	Translation initiation factor eif-2B subunit alpha	protein	291	46% helix, 10% strand	Q14232
C	Translation initiation factor eif-2B subunit beta	protein	317	47% helix, 14% strand	P49770
D	Translation initiation factor eif-2B subunit beta	protein	324	46% helix, 14% strand	P49770
E	Translation initiation factor eif-2B subunit gamma	protein	346	21% helix, 18% strand	Q9NR50
F	Translation initiation factor eif-2B subunit gamma	protein	350	21% helix, 21% strand	Q9NR50
G, H	Translation initiation factor eif-2B subunit delta	protein	353	41% helix, 12% strand	Q9UI10
I	Translation initiation factor eif-2B subunit epsilon	protein	427	20% helix, 20% strand	Q13144
J	Translation initiation factor eif-2B subunit epsilon	protein	429	21% helix, 16% strand	Q13144
K	Eukaryotic translation initiation factor 2 subunit 1	protein	176	38% helix, 19% strand	P05198

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	1024	0.86	0.87	97	empty
2	908	0.86	0.88	110	empty
3	1140	0.82	0.83	134	empty
4	977	0.80	0.81	87	empty
5	712	0.79	0.84	80	empty

Interfaces

24 interfaces between chains.

C–G · 2247 Å² buried · 26 hydrogen bonds · protein-protein
D–H · 2208 Å² buried · 18 hydrogen bonds · protein-protein
C–I · 1430 Å² buried · 10 hydrogen bonds · protein-protein
A–B · 1369 Å² buried · 17 hydrogen bonds · protein-protein
D–J · 1317 Å² buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (phosphorylation).

Compared structures

7D45 · eIF2B-eIF2(aP), aP1 complex · the same entry in another collection · chain K against K, TM-score 1.00
Q9UI10 · AlphaFold monomer V2.0 prediction for translation initiation factor eif-2B subunit delta… · a predicted model of the same protein · chain H against A, TM-score 0.98

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
Elsewhere: RCSB PDB 7D45 · PDBe 7D45 · UniProt Q14232 · UniProt P49770 · UniProt Q9NR50 · UniProt Q9UI10 · UniProt Q13144 · UniProt P05198

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