MolNFT v1 · #144492 · protein

Crystal structure of AAC(3)-ia in complex with coenzyme a

6BVC · Aminoglycoside-(3)-N-acetyltransferase: “Crystal structure of AAC(3)-ia in complex with coenzyme a”. X-ray diffraction, 2 ligands (COA, CL), 3 pockets (best druggability 0.55). MolNFT v1 #144492 on GenesisL1: 3D structure, binding…

PDB: 6BVC
Type: protein
Length: 154 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aminoglycoside-(3)-N-acetyltransferase
UniProt: Q53396
Ligands: COA, CL
Pockets: 3 · best druggability 0.55

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Aminoglycoside-(3)-N-acetyltransferase	protein	154	42% helix, 25% strand	Q53396

Ligands and binding sites

COA · Coenzyme A · ligand · chains A
CL · Chloride ion · ion · chains A
GOL · Glycerol · additive · 3 copies · chains A
PE3 · 3,6,9,12,15,18,21,24,27,30,33,36,39-tridecaoxahentetracontane-1,41-diol · additive · 2 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	222	0.55	0.78	22	empty
2	242	0.54	0.77	30	COA, GOL
3	106	0.45	0.78	16	empty

Compared structures

6BVC · Crystal structure of AAC(3)-Ia in complex with coenzyme A · 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 Q53396
Elsewhere: RCSB PDB 6BVC · PDBe 6BVC · UniProt Q53396

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