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Non-structural protein 10 (NSP10) from SARS cov-2 in complex with fragment VT00239

Analyse Non-structural protein 10 (NSP10) from SARS cov-2 in complex with fragment… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7ORV
Type: protein
Length: 124 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Non-structural protein 10
UniProt: P0DTD1
Ligands: X4V, ZN, CL
Pockets: 1 · best druggability 0.38

Structure

x-ray diffraction · 1 distinct chain · 29% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Non-structural protein 10	protein	124	29% helix, 12% strand	P0DTD1

Ligands and binding sites

X4V · N~4~,N~4~-dimethylpyridine-2,4-diamine · ligand · chains A
ZN · Zinc ion · metal · 2 copies · chains A
CL · Chloride ion · ion · 3 copies · chains A
DMS · Dimethyl sulfoxide · additive · 2 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	74	0.38	0.77	17	empty

Compared structures

7ORV · Non-structural protein 10 (nsp10) from SARS CoV-2 in complex with fragment VT00239 · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P0DTD1
Elsewhere: RCSB PDB 7ORV · PDBe 7ORV · UniProt P0DTD1

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