Research workbench

Crystal structure of dimeric R298A mutant of SARS coronavirus main protease

Analyse Crystal structure of dimeric R298A mutant of 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: 4HI3
Type: protein
Length: 601 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 3C-like proteinase
EC: 3.4.22.-
UniProt: P0C6U8
Pockets: 7 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 26% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	3C-like proteinase (EC 3.4.22.-)	protein	300	26% helix, 30% strand	P0C6U8
B	3C-like proteinase (EC 3.4.22.-)	protein	301	26% helix, 30% strand	P0C6U8

Pockets

7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	997	0.76	0.78	84	empty
2	278	0.56	0.77	44	empty
3	245	0.54	0.77	35	empty
4	170	0.47	0.76	28	empty
5	114	0.37	0.74	27	empty

Interfaces

1 interface between chains.

A–B · 1283 Å² buried · 34 hydrogen bonds · protein-protein

Compared structures

4HI3 · Crystal structure of dimeric R298A mutant of 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 4HI3 · PDBe 4HI3 · UniProt P0C6U8

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.