MolNFT v1 · #47679 · protein

Crystal structure analysis of the west nile virus envelope (E) protein domain III

2P5P · Genome polyprotein: “Crystal structure analysis of the west nile virus envelope (E) protein domain III”. X-ray diffraction, 4 pockets (best druggability 0.76). MolNFT v1 #47679 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 2P5P
Type: protein
Length: 303 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Genome polyprotein
UniProt: P06935
Pockets: 4 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 0% helix, 52% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Genome polyprotein	protein	101	0% helix, 52% strand	P06935

Pockets

4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	89	0.76	0.97	27	empty
2	100	0.51	0.82	23	empty
3	99	0.50	0.82	21	empty
4	118	0.40	0.75	25	empty

Interfaces

3 interfaces between chains.

A–C · 696 Å² buried · 11 hydrogen bonds · protein-protein
A–B · 517 Å² buried · 8 hydrogen bonds · protein-protein
B–C · 163 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

2P5P · Crystal Structure Analysis of the West Nile virus envelope (E) protein domain III · 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 P06935
Elsewhere: RCSB PDB 2P5P · PDBe 2P5P · UniProt P06935

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