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Crystallographic and biochemical analysis of rotavirus NSP2 with nucleotides reveals an ndp kinase like activity

Analyse Crystallographic and biochemical analysis of rotavirus NSP2 with nucleotides… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2R7C
Type: protein
Length: 308 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Non-structural RNA-binding protein 35
UniProt: Q03243
Ligands: PO4
Pockets: 2 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Non-structural RNA-binding protein 35	protein	308	40% helix, 16% strand	Q03243

Ligands and binding sites

PO4 · Phosphate ion · ion · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	592	0.66	0.76	52	empty
2	195	0.48	0.75	22	empty

Modifications

Observed in the structure: 1 modified (nonstandard).

Compared structures

2R7C · Crystallographic and biochemical analysis of rotavirus NSP2 with nucleotides reveals an… · 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 Q03243
Elsewhere: RCSB PDB 2R7C · PDBe 2R7C · UniProt Q03243

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