› 7kps

X-ray diffraction
1.8Å resolution

Structure of a GNAT superfamily PA3944 acetyltransferase in complex with AcCoA

Released:
DOI: 10.2210/pdb7kps/pdb
Model geometry
Fit model/data
PDB entry 7kps coloured by chain, front view.
PDB entry 7kps coloured by chain, side view.
PDB entry 7kps coloured by chain, top view.
Source organism: Pseudomonas aeruginosa
Primary publication:
Gcn5-Related N-Acetyltransferases (GNATs) With a Catalytic Serine Residue Can Play Ping-Pong Too.
Baumgartner JT, Habeeb Mohammad TS, Czub MP, Majorek KA, Arolli X, Variot C, Anonick M, Minor W, Ballicora MA, Becker DP, Kuhn ML
OpenAccess logo Front Mol Biosci 8 646046 (2021)
PMID: 33912589

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-191097 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Acetyltransferase PA3944 Chain: A
Molecule details ›
Chain: A
Length: 194 amino acids
Theoretical weight: 22.1 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9HX72 (Residues: 1-192; Coverage: 100%)
Gene name: PA3944
Sequence domains: Acetyltransferase (GNAT) domain
Acetyltransferase PA3944 Chain: B
Molecule details ›
Chain: B
Length: 194 amino acids
Theoretical weight: 22.08 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9HX72 (Residues: 1-192; Coverage: 100%)
Gene name: PA3944
Sequence domains: Acetyltransferase (GNAT) domain

Ligands and Environments

6 bound ligands:
Ligand COA 1 x COA
Ligand EDO 4 x EDO
Ligand TRS 2 x TRS
Ligand ACO 1 x ACO
Ligand PEG 2 x PEG
Ligand PGE 1 x PGE
1 modified residue:
Ligand CSX 1 x CSX

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: P1
Unit cell:
a: 36.563Å b: 44.246Å c: 60.183Å
α: 97.94° β: 106.72° γ: 89.92°
R-values:
R R work R free
0.208 0.206 0.235
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Post-translational Lysine Ac(et)ylation in Bacteria: A Biochemical, Structural, and Synthetic Biological Perspective.
Lammers M. (2021)
1 more

2 mentions without citation

Gcn5-Related N-Acetyltransferases (GNATs) With a Catalytic Serine Residue Can Play Ping-Pong Too.
Baumgartner et al. (2021)
1 more