Research workbench

Crystal structure of the type B chloramphenicol acetyltransferase from vibrio cholerae in the complex with crystal violet

Analyse Crystal structure of the type B chloramphenicol acetyltransferase from vibrio… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6PUB
Type: protein
Length: 210 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Chloramphenicol acetyltransferase
UniProt: Q9KMN1
Ligands: CVI, SO4, CL
Pockets: 2 · best druggability 0.42

Structure

x-ray diffraction · 1 distinct chain · 25% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Chloramphenicol acetyltransferase	protein	210	25% helix, 19% strand	Q9KMN1

Ligands and binding sites

CVI · Crystal violet · ligand · chains A
SO4 · Sulfate ion · ion · 8 copies · chains A
CL · Chloride ion · ion · 5 copies · 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	89	0.42	0.78	17	empty
2	76	0.36	0.76	15	empty

Compared structures

6PUB · Crystal Structure of the Type B Chloramphenicol Acetyltransferase from Vibrio cholerae in… · 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 Q9KMN1
Elsewhere: RCSB PDB 6PUB · PDBe 6PUB · UniProt Q9KMN1

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