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Crystal structure of aminoglycoside N-acetyltransferase AAC(6')-IB11

Analyse Crystal structure of aminoglycoside N-acetyltransferase AAC(6')-IB11 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2PR8
Type: protein
Length: 346 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aminoglycoside 6-N-acetyltransferase type IB11
EC: 2.3.1.82
UniProt: Q8GLI5
Pockets: 4 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Aminoglycoside 6-N-acetyltransferase type IB11 (EC 2.3.1.82)	protein	173	27% helix, 29% strand	Q8GLI5

Ligands and binding sites

EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	110	0.61	0.87	35	empty
2	435	0.59	0.75	55	EPE
3	230	0.48	0.74	30	EPE
4	79	0.38	0.77	14	empty

Interfaces

1 interface between chains.

A–B · 959 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

2PR8 · crystal structure of aminoglycoside N-acetyltransferase AAC(6')-Ib11 · 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 Q8GLI5
Elsewhere: RCSB PDB 2PR8 · PDBe 2PR8 · UniProt Q8GLI5

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