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The crystal structure of papain-like protease of SARS cov-2 , C111S mutant

Analyse The crystal structure of papain-like protease of SARS cov-2 , C111S mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6WRH
Type: protein
Length: 316 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Non-structural protein 3
EC: 3.4.19.121, 3.4.22.-
UniProt: P0DTD1
Ligands: ZN, PO4, CL
Pockets: 2 · best druggability 0.42

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Non-structural protein 3 (EC 3.4.19.121, 3.4.22.-)	protein	316	26% helix, 36% strand	P0DTD1

Ligands and binding sites

ZN · Zinc ion · metal · chains A
PO4 · Phosphate ion · ion · 3 copies · chains A
CL · Chloride ion · ion · 2 copies · chains A
GOL · Glycerol · additive · 2 copies · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	51	0.42	0.82	12	empty
2	65	0.36	0.78	18	empty

Compared structures

6WRH · The crystal structure of Papain-Like Protease of SARS CoV-2 , C111S mutant · 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 P0DTD1
Elsewhere: RCSB PDB 6WRH · PDBe 6WRH · UniProt P0DTD1

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