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Crystal structure of virus-like particle from pyrococcus furiosus

Analyse Crystal structure of virus-like particle from pyrococcus furiosus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2E0Z
Type: protein
Length: 700 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Virus-like particle
UniProt: Q401P1
Pockets: 7 · best druggability 0.74

Structure

x-ray diffraction · 2 distinct chains · 34% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Virus-like particle	protein	236	34% helix, 33% strand	Q401P1
C	Virus-like particle	protein	228	33% helix, 34% strand	Q401P1

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	681	0.74	0.80	64	empty
2	314	0.55	0.76	46	empty
3	109	0.45	0.79	32	empty
4	63	0.41	0.80	17	empty
5	61	0.37	0.79	16	empty

Interfaces

3 interfaces between chains.

A–B · 1419 Å² buried · 14 hydrogen bonds · protein-protein
B–C · 403 Å² buried · 6 hydrogen bonds · protein-protein
A–C · 280 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

2E0Z · Crystal structure of virus-like particle from Pyrococcus furiosus · 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 Q401P1
Elsewhere: RCSB PDB 2E0Z · PDBe 2E0Z · UniProt Q401P1

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