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Product state mimicry leads to aminoglycoside discrimination in an antibiotic acetyltransferase

Analyse Product state mimicry leads to aminoglycoside discrimination in an antibiotic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6NP1
Type: protein
Length: 268 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aminoglycoside N(3)-acetyltransferase
EC: 2.3.1.81
UniProt: Q47030
Ligands: MG
Pockets: 1 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Aminoglycoside N(3)-acetyltransferase (EC 2.3.1.81)	protein	268	37% helix, 21% strand	Q47030

Ligands and binding sites

MG · Magnesium ion · metal · 2 copies · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	306	0.59	0.78	40	empty

Compared structures

6NP1 · Product state mimicry leads to aminoglycoside discrimination in an antibiotic… · 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 Q47030
Elsewhere: RCSB PDB 6NP1 · PDBe 6NP1 · UniProt Q47030

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