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X-ray crystal structure of the SARS coronavirus main protease

Analyse X-ray crystal structure of the SARS coronavirus main protease in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1Q2W
Type: protein
Length: 592 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 3C-like protease
EC: 3.4.22.-
UniProt: P0C6U8
Pockets: 6 · best druggability 0.75

Structure

x-ray diffraction · 2 distinct chains · 25% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	3C-like protease (EC 3.4.22.-)	protein	295	25% helix, 29% strand	P0C6U8
B	3C-like protease (EC 3.4.22.-)	protein	297	25% helix, 30% strand	P0C6U8

Ligands and binding sites

MPD · (4S)-2-methyl-2,4-pentanediol · additive · chains A

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	994	0.75	0.78	82	empty
2	543	0.63	0.75	75	empty
3	183	0.49	0.76	29	empty
4	126	0.40	0.74	25	empty
5	87	0.37	0.76	18	MPD

Interfaces

1 interface between chains.

A–B · 1094 Å² buried · 25 hydrogen bonds · protein-protein

Compared structures

1Q2W · X-Ray Crystal Structure of the SARS Coronavirus Main Protease · 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 P0C6U8
Elsewhere: RCSB PDB 1Q2W · PDBe 1Q2W · UniProt P0C6U8

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