Research workbench

Crystal structure of bleomycin N-acetyltransferase complexed with coenzyme a in the trigonal crystal

Analyse Crystal structure of bleomycin N-acetyltransferase complexed with coenzyme a in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2ZW5
Type: protein
Length: 586 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Bleomycin acetyltransferase
UniProt: Q53796
Ligands: COA
Pockets: 4 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 25% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Bleomycin acetyltransferase	protein	293	25% helix, 36% strand	Q53796

Ligands and binding sites

COA · Coenzyme A · ligand · 2 copies · chains A, B

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

Pockets

4 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	875	0.81	0.84	94	empty
2	449	0.74	0.83	52	COA
3	418	0.72	0.83	50	COA
4	60	0.41	0.81	18	empty

Interfaces

1 interface between chains.

A–B · 2520 Å² buried · 27 hydrogen bonds · protein-protein

Compared structures

2ZW5 · Crystal structure of bleomycin N-acetyltransferase complexed with coenzyme A in the… · 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 Q53796
Elsewhere: RCSB PDB 2ZW5 · PDBe 2ZW5 · UniProt Q53796

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