Research workbench

SARS-cov-2 main protease C145S mutant in complex with N and C-terminal residues

Analyse SARS-cov-2 main protease C145S mutant in complex with N and C-terminal residues in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7N6N
Type: protein
Length: 617 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 3C-like proteinase
EC: 3.4.22.69
UniProt: P0DTD1
Pockets: 7 · best druggability 0.70

Structure

x-ray diffraction · 2 distinct chains · 24% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	3C-like proteinase (EC 3.4.22.69)	protein	306	24% helix, 28% strand	P0DTD1
C	3C-like proteinase	protein	5	0% helix, 40% strand	P0DTD1

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	664	0.70	0.78	59	empty
2	313	0.62	0.79	43	empty
3	199	0.50	0.76	29	empty
4	140	0.42	0.75	24	empty
5	87	0.34	0.74	18	empty

Interfaces

3 interfaces between chains.

A–B · 1543 Å² buried · 37 hydrogen bonds · protein-protein
A–C · 516 Å² buried · 15 hydrogen bonds · protein-protein
B–C · 24 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

7N6N · SARS-CoV-2 Main protease C145S mutant in complex with N and C-terminal residues · 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 7N6N · PDBe 7N6N · UniProt P0DTD1

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