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Crystal structure of P domain of hawaii norovirus (GII.1)

Analyse Crystal structure of P domain of hawaii norovirus (GII.1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4ROX
Type: protein
Length: 598 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Capsid protein VP1
UniProt: J9XXB7
Pockets: 7 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 6% helix, 37% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Capsid protein VP1	protein	299	6% helix, 37% strand	J9XXB7

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 7 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	91	0.76	0.98	27	empty
2	104	0.72	0.93	20	EDO
3	247	0.60	0.80	36	empty
4	254	0.59	0.80	37	empty
5	113	0.41	0.76	22	EDO

Interfaces

1 interface between chains.

A–B · 1817 Å² buried · 27 hydrogen bonds · protein-protein

Compared structures

4ROX · Crystal Structure of P Domain of Hawaii Norovirus (GII.1) · 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 J9XXB7
Elsewhere: RCSB PDB 4ROX · PDBe 4ROX · UniProt J9XXB7

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