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Crystal structure of human EIF2B alpha

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

PDB: 3ECS
Type: protein
Length: 2,286 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Translation initiation factor eif-2B subunit alpha
UniProt: Q14232
Ligands: SO4, CL
Pockets: 20 · best druggability 0.70

Structure

x-ray diffraction · 8 distinct chains · 49% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Translation initiation factor eif-2B subunit alpha	protein	279	51% helix, 15% strand	Q14232
B	Translation initiation factor eif-2B subunit alpha	protein	281	51% helix, 15% strand	Q14232
C	Translation initiation factor eif-2B subunit alpha	protein	294	51% helix, 15% strand	Q14232
D	Translation initiation factor eif-2B subunit alpha	protein	291	49% helix, 14% strand	Q14232
E	Translation initiation factor eif-2B subunit alpha	protein	285	47% helix, 15% strand	Q14232
F	Translation initiation factor eif-2B subunit alpha	protein	287	50% helix, 15% strand	Q14232
G	Translation initiation factor eif-2B subunit alpha	protein	284	49% helix, 15% strand	Q14232
H	Translation initiation factor eif-2B subunit alpha	protein	285	48% helix, 14% strand	Q14232

Ligands and binding sites

SO4 · Sulfate ion · ion · 10 copies · chains A, F, B, C, D, E, G, H
CL · Chloride ion · ion · chains A

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

Pockets

20 pockets found on a 1 Å grid, 18 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	314	0.70	0.84	31	SO4
2	661	0.69	0.77	74	SO4
3	340	0.67	0.81	36	SO4
4	330	0.66	0.81	37	SO4
5	443	0.66	0.78	47	empty

Interfaces

12 interfaces between chains.

D–E · 1891 Å² buried · 42 hydrogen bonds · protein-protein
A–C · 1871 Å² buried · 35 hydrogen bonds · protein-protein
F–G · 1749 Å² buried · 32 hydrogen bonds · protein-protein
B–H · 1598 Å² buried · 29 hydrogen bonds · protein-protein
A–B · 778 Å² buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 56 modified (engineered).

Compared structures

3ECS · Crystal structure of human eIF2B alpha · the same entry in another collection · chain H against H, TM-score 1.00
Q14232 · AlphaFold monomer V2.0 prediction for translation initiation factor eif-2B subunit alpha… · a predicted model of the same protein · chain A against A, TM-score 0.97

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
Elsewhere: RCSB PDB 3ECS · PDBe 3ECS · UniProt Q14232

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