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Crystal structures of the SARS-coronavirus main proteinase inactivated by benzotriazole compounds

Analyse Crystal structures of the SARS-coronavirus main proteinase inactivated by… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2V6N
Type: protein
Length: 306 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Replicase polyprotein 1AB
EC: 3.4.24.-
UniProt: Q6WGN0
Ligands: XP1, SO4
Pockets: 2 · best druggability 0.50

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Replicase polyprotein 1AB (EC 3.4.24.-)	protein	306	24% helix, 28% strand	Q6WGN0

Ligands and binding sites

XP1 · 4-(dimethylamino)benzoic acid · ligand · chains A
SO4 · Sulfate ion · ion · chains A
MES · 2-(N-morpholino)-ethanesulfonic acid · additive · chains A

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	189	0.50	0.77	26	XP1
2	114	0.40	0.75	25	empty

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

2V6N · Crystal structures of the SARS-coronavirus main proteinase inactivated by benzotriazole… · 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 Q6WGN0
Elsewhere: RCSB PDB 2V6N · PDBe 2V6N · UniProt Q6WGN0

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