Research workbench

Room temperature X-ray crystallography reveals oxidation and reactivity of cysteine residues in SARS-cov-2 3CL mpro: insights for enzyme mechanism and drug design

Analyse Room temperature X-ray crystallography reveals oxidation and reactivity of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

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

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	3C-like proteinase (EC 3.4.22.69)	protein	306	26% helix, 29% strand	P0DTD1

Pockets

6 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	999	0.77	0.79	74	empty
2	372	0.57	0.75	49	empty
3	213	0.52	0.77	28	empty
4	202	0.50	0.76	28	empty
5	213	0.49	0.75	32	empty

Interfaces

1 interface between chains.

A–C · 1630 Å² buried · 44 hydrogen bonds · protein-protein

Compared structures

6XHU · Room temperature X-ray crystallography reveals oxidation and reactivity of cysteine… · 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 6XHU · PDBe 6XHU · UniProt P0DTD1

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