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Crystallographic structure of apo human rotavirus K8 VP8*

Analyse Crystallographic structure of apo human rotavirus K8 VP8* in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5CAZ
Type: protein
Length: 161 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Outer capsid protein VP4
UniProt: Q01641
Ligands: SO4
Pockets: 1 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 8% helix, 56% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Outer capsid protein VP4	protein	161	8% helix, 56% strand	Q01641

Ligands and binding sites

SO4 · Sulfate ion · ion · chains A
IPA · Isopropyl alcohol · additive · 7 copies · chains A
GOL · Glycerol · additive · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	61	0.74	1.00	21	empty

Compared structures

5CAZ · Crystallographic structure of apo human rotavirus K8 VP8* · 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 Q01641
Elsewhere: RCSB PDB 5CAZ · PDBe 5CAZ · UniProt Q01641

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