› 7zhc

X-ray diffraction
1.82Å resolution

Moss spermine/spermidine acetyl transferase (PpSSAT) in complex with AcetylCoA and polyethylen glycol

Released:
DOI: 10.2210/pdb7zhc/pdb
Model geometry
Fit model/data
PDB entry 7zhc coloured by chain, front view.
PDB entry 7zhc coloured by chain, side view.
PDB entry 7zhc coloured by chain, top view.
Source organism: Physcomitrium patens
Primary publication:
Biochemical and structural basis of polyamine, lysine and ornithine acetylation catalyzed by spermine/spermidine N-acetyl transferase in moss and maize.
Bělíček J, Ľuptáková E, Kopečný D, Frömmel J, Vigouroux A, Ćavar Zeljković S, Jagic F, Briozzo P, Kopečný DJ, Tarkowski P, Nisler J, De Diego N, Moréra S, Kopečná M
Plant J (2023)
PMID: 36786691

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-215299 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N-acetyltransferase domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 234 amino acids
Theoretical weight: 26.1 KDa
Source organism: Physcomitrium patens
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'
UniProt:
  • Canonical: A0A2K1KKM6 (Residues: 1-214; Coverage: 100%)
Gene name: PHYPA_008003
Sequence domains: Acetyltransferase (GNAT) family

Ligands and Environments

3 bound ligands:
Ligand ACO 2 x ACO
Ligand GOL 1 x GOL
Ligand 1PE 1 x 1PE
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: SOLEIL BEAMLINE PROXIMA 2
Spacegroup: P21
Unit cell:
a: 48.108Å b: 97.773Å c: 48.453Å
α: 90° β: 117.4° γ: 90°
R-values:
R R work R free
0.202 0.199 0.234
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'

Quick links

Citations

1 citations in other articles

Crystal structure of a GCN5-related N-acetyltransferase from Lactobacillus curiae.
Fleming et al. (2023)