Research workbench

Asymmetric focsued reconstruction of human norovirus GII.2 snow mountain virus strain vlp asymmetric unit in T=1 symmetry

Analyse Asymmetric focsued reconstruction of human norovirus GII.2 snow mountain virus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6OUC
Type: protein
Length: 483 residues
Chains: 1
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Viral protein 1
UniProt: Q80RD6
Ligands: ZN
Pockets: 2 · best druggability 0.58

Structure

electron microscopy · 1 distinct chain · 5% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Viral protein 1	protein	483	5% helix, 34% strand	Q80RD6

Ligands and binding sites

ZN · Zinc ion · metal · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	254	0.58	0.79	33	empty
2	144	0.54	0.81	26	empty

Compared structures

6OUC · Asymmetric focsued reconstruction of human norovirus GII.2 Snow Mountain Virus strain VLP… · 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 Q80RD6
Elsewhere: RCSB PDB 6OUC · PDBe 6OUC · UniProt Q80RD6

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.