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Crystal structure of eukaryotic initiation factor 4E from pisum sativum

Analyse Crystal structure of eukaryotic initiation factor 4E from pisum sativum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2WMC
Type: protein
Length: 1,337 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Eukaryotic translation initiation factor 4E
UniProt: Q6TEC4
Ligands: MGP
Pockets: 20 · best druggability 0.79

Structure

x-ray diffraction · 8 distinct chains · 27% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Eukaryotic translation initiation factor 4E	protein	174	28% helix, 32% strand	Q6TEC4
B	Eukaryotic translation initiation factor 4E	protein	159	28% helix, 35% strand	Q6TEC4
C	Eukaryotic translation initiation factor 4E	protein	172	30% helix, 31% strand	Q6TEC4
D	Eukaryotic translation initiation factor 4E	protein	163	29% helix, 33% strand	Q6TEC4
E	Eukaryotic translation initiation factor 4E	protein	167	30% helix, 33% strand	Q6TEC4
F	Eukaryotic translation initiation factor 4E	protein	162	25% helix, 34% strand	Q6TEC4
G	Eukaryotic translation initiation factor 4E	protein	169	22% helix, 33% strand	Q6TEC4
H	Eukaryotic translation initiation factor 4E	protein	171	26% helix, 32% strand	Q6TEC4

Ligands and binding sites

MGP · 7-methyl-guanosine-5'-triphosphate · ligand · 8 copies · chains A, B, 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, 8 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	862	0.79	0.82	86	empty
2	826	0.74	0.79	79	empty
3	223	0.69	0.85	22	empty
4	341	0.65	0.80	32	empty
5	411	0.61	0.76	40	empty

Interfaces

14 interfaces between chains.

G–H · 703 Å² buried · 8 hydrogen bonds · protein-protein
B–C · 674 Å² buried · 9 hydrogen bonds · protein-protein
C–D · 643 Å² buried · 10 hydrogen bonds · protein-protein
E–H · 630 Å² buried · 6 hydrogen bonds · protein-protein
A–D · 619 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

2WMC · Crystal structure of eukaryotic initiation factor 4E from Pisum sativum · the same entry in another collection · chain A against A, 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 Q6TEC4
Elsewhere: RCSB PDB 2WMC · PDBe 2WMC · UniProt Q6TEC4

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