MolNFT v1 · #182253 · protein

Crystal structure of SARS-cov-2 main protease (3CLPRO/MPRO) covalently bound to compound C63

7MLG · 3C-like proteinase: “Crystal structure of SARS-cov-2 main protease (3CLPRO/MPRO) covalently bound to compound C63”. X-ray diffraction, 1 ligand (ZJ1), 3 pockets (best druggability 0.54). MolNFT v1 #182253 on GenesisL1: 3D structure…

PDB: 7MLG
Type: protein
Length: 304 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 3C-like proteinase
EC: 3.4.22.69
UniProt: P0DTD1
Ligands: ZJ1
Pockets: 3 · best druggability 0.54

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	3C-like proteinase (EC 3.4.22.69)	protein	304	26% helix, 28% strand	P0DTD1

Ligands and binding sites

ZJ1 · (2R)-2-[(4-tert-butylphenyl)(ethanesulfonyl)amino]-N-cyclohexyl-2-(pyridin-3-yl)acetamide · ligand · chains A

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

Pockets

3 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	237	0.54	0.77	28	ZJ1
2	98	0.37	0.75	17	empty
3	100	0.37	0.74	16	empty

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

7MLG · Crystal Structure of SARS-CoV-2 Main Protease (3CLpro/Mpro) Covalently Bound to Compound… · 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 7MLG · PDBe 7MLG · UniProt P0DTD1

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