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

Analyse Crystal structure analysis of the west nile virus envelope (E) protein domain… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

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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