Research workbench

EIF2B APO

Analyse EIF2B APO in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7D46
Type: protein
Length: 3,481 residues
Chains: 10
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
Pockets: 20 · best druggability 0.87

Structure

electron microscopy · 8 distinct chains · 34% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Translation initiation factor eif-2B subunit alpha	protein	293	46% helix, 9% strand	Q14232
B	Translation initiation factor eif-2B subunit alpha	protein	291	47% helix, 8% strand	Q14232
C	Translation initiation factor eif-2B subunit beta	protein	321	43% helix, 6% strand	P49770
D	Translation initiation factor eif-2B subunit beta	protein	324	47% helix, 10% strand	P49770
E, F	Translation initiation factor eif-2B subunit gamma	protein	345	20% helix, 17% strand	Q9NR50
G, H	Translation initiation factor eif-2B subunit delta	protein	353	40% helix, 11% 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	21% helix, 17% strand	Q13144

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	1063	0.87	0.88	107	empty
2	1039	0.87	0.88	105	empty
3	678	0.81	0.86	78	empty
4	573	0.81	0.87	75	empty
5	913	0.76	0.79	76	empty

Interfaces

22 interfaces between chains.

D–H · 2189 Å² buried · 19 hydrogen bonds · protein-protein
C–G · 2183 Å² buried · 17 hydrogen bonds · protein-protein
A–B · 1448 Å² buried · 21 hydrogen bonds · protein-protein
C–I · 1418 Å² buried · 7 hydrogen bonds · protein-protein
D–J · 1335 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

7D46 · eIF2B apo · the same entry in another collection · chain J against J, 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
Elsewhere: RCSB PDB 7D46 · PDBe 7D46 · UniProt Q14232 · UniProt P49770 · UniProt Q9NR50 · UniProt Q9UI10 · UniProt Q13144

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