MolNFT v1 · #190966 · protein

Crystal structure of SARS-cov-2 main protease (mpro) variant C44S at 2.12 a resolution

7ZB6 · 3C-like proteinase NSP5: “Crystal structure of SARS-cov-2 main protease (mpro) variant C44S at 2.12 a resolution”. X-ray diffraction, 6 pockets (best druggability 0.77). MolNFT v1 #190966 on GenesisL1: 3D structure, binding sites…

PDB: 7ZB6
Type: protein
Length: 612 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 3C-like proteinase NSP5
EC: 3.4.22.69
UniProt: P0DTD1
Pockets: 6 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 24% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	3C-like proteinase NSP5 (EC 3.4.22.69)	protein	306	24% helix, 28% strand	P0DTD1

Ligands and binding sites

DMS · Dimethyl sulfoxide · additive · chains C

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

Pockets

6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1192	0.77	0.79	86	empty
2	406	0.56	0.74	52	empty
3	182	0.46	0.75	26	empty
4	129	0.42	0.76	18	empty
5	132	0.41	0.75	18	empty

Interfaces

1 interface between chains.

A–C · 1535 Å² buried · 39 hydrogen bonds · protein-protein

Compared structures

7ZB6 · Crystal Structure of SARS-CoV-2 Main Protease (Mpro) variant C44S at 2.12 A resolution · 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 7ZB6 · PDBe 7ZB6 · UniProt P0DTD1

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