MolNFT v1 · #153681 · protein

EIF2A - EIF2B complex

6JLY · Translation initiation factor eif-2B subunit alpha: “EIF2A - EIF2B complex”. X-ray diffraction, 1 ligand (PO4), 20 pockets (best druggability 0.85). MolNFT v1 #153681 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6JLY
Type: protein
Length: 4,044 residues
Chains: 12
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Translation initiation factor eif-2B subunit alpha; Probable translation initiation…
UniProt: Q9USP0, Q9UT76, P56288, Q09924, P56287, P20459
Ligands: PO4
Pockets: 20 · best druggability 0.85

Structure

x-ray diffraction · 11 distinct chains · 33% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Translation initiation factor eif-2B subunit alpha	protein	316	47% helix, 12% strand	Q9USP0
B	Translation initiation factor eif-2B subunit alpha	protein	316	46% helix, 13% strand	Q9USP0
C	Probable translation initiation factor eif-2B subunit beta	protein	338	51% helix, 14% strand	Q9UT76
D	Probable translation initiation factor eif-2B subunit beta	protein	337	51% helix, 14% strand	Q9UT76
E	Probable translation initiation factor eif-2B subunit gamma	protein	414	19% helix, 24% strand	P56288
F	Probable translation initiation factor eif-2B subunit gamma	protein	412	21% helix, 24% strand	P56288
G, H	Probable translation initiation factor eif-2B subunit delta	protein	363	43% helix, 12% strand	Q09924
I	Probable translation initiation factor eif-2B subunit epsilon	protein	428	20% helix, 25% strand	P56287
J	Probable translation initiation factor eif-2B subunit epsilon	protein	426	21% helix, 26% strand	P56287
L	Eukaryotic translation initiation factor 2 subunit alpha	protein	165	25% helix, 22% strand	P20459
M	Eukaryotic translation initiation factor 2 subunit alpha	protein	166	31% helix, 20% strand	P20459

Ligands and binding sites

PO4 · Phosphate ion · ion · 8 copies · chains C, D, E, F, G, H

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

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	545	0.85	0.91	81	empty
2	963	0.82	0.83	83	empty
3	349	0.79	0.89	60	empty
4	893	0.78	0.81	79	empty
5	767	0.78	0.82	74	empty

Interfaces

28 interfaces between chains.

A–B · 3281 Å² buried · 33 hydrogen bonds · protein-protein
D–H · 2365 Å² buried · 21 hydrogen bonds · protein-protein
C–G · 2362 Å² buried · 20 hydrogen bonds · protein-protein
D–J · 1499 Å² buried · 19 hydrogen bonds · protein-protein
C–I · 1495 Å² buried · 15 hydrogen bonds · protein-protein

Compared structures

6JLY · eIF2a - eIF2B complex · the same entry in another collection · chain M against M, 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 Q9USP0
Every structure of UniProt Q9UT76
Every structure of UniProt P56288
Every structure of UniProt Q09924
Every structure of UniProt P56287
Every structure of UniProt P20459
Elsewhere: RCSB PDB 6JLY · PDBe 6JLY · UniProt Q9USP0 · UniProt Q9UT76 · UniProt P56288 · UniProt Q09924 · UniProt P56287 · UniProt P20459

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