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Crystal structure of human rotavirus NSP2 (group C / bristol strain)

Analyse Crystal structure of human rotavirus NSP2 (group C / bristol strain) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2GU0
Type
protein
Length
602 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Nonstructural protein 2
UniProt
Q9PY93
Pockets
5 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BNonstructural protein 2protein30147% helix, 16% strandQ9PY93

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13550.590.7645empty
23450.560.7532empty
31320.540.8222empty
41420.540.8126empty
5520.260.7416empty

Interfaces

1 interface between chains.

  • A–B · 120 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 2GU0 · Crystal Structure of Human Rotavirus NSP2 (Group C / Bristol Strain) · the same entry in another collection · chain A against A, TM-score 1.00

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