MolNFT v1 · #138186 · protein

Leishmania IF4E-1 bound to leishmania 4E-IP1

5WB5 · Putative eukaryotic translation initiation factor eif-4E: “Leishmania IF4E-1 bound to leishmania 4E-IP1”. X-ray diffraction, 2 pockets (best druggability 0.43). MolNFT v1 #138186 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 5WB5
Type: protein
Length: 207 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative eukaryotic translation initiation factor eif-4E; Uncharacterized protein
UniProt: E9ADE1, E9AFM3
Pockets: 2 · best druggability 0.43

Structure

x-ray diffraction · 2 distinct chains · 33% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative eukaryotic translation initiation factor eif-4E	protein	167	29% helix, 34% strand	E9ADE1
B	Uncharacterized protein	protein	40	50% helix, 3% strand	E9AFM3

Ligands and binding sites

PEG · Di(hydroxyethyl)ether · additive · chains A

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	169	0.43	0.74	28	empty
2	75	0.40	0.78	19	empty

Interfaces

1 interface between chains.

A–B · 1507 Å² buried · 23 hydrogen bonds · protein-protein

Compared structures

5WB5 · Leishmania IF4E-1 bound to Leishmania 4E-IP1 · 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 E9ADE1
Every structure of UniProt E9AFM3
Elsewhere: RCSB PDB 5WB5 · PDBe 5WB5 · UniProt E9ADE1 · UniProt E9AFM3

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