› 6sse

X-ray diffraction
1.56Å resolution

Transaminase with PMP bound

Released:
DOI: 10.2210/pdb6sse/pdb
PDB entry 6sse coloured by chain, front view.
PDB entry 6sse coloured by chain, side view.
PDB entry 6sse coloured by chain, top view.
Source organism: Streptomyces kaniharaensis
Primary publication:
PMP-diketopiperazine adducts form at the active site of a PLP dependent enzyme involved in formycin biosynthesis.
Gao S, Liu H, de Crécy-Lagard V, Zhu W, Richards NGJ, Naismith JH
Chem Commun (Camb) 55 14502-14505 (2019)
PMID: 31730149

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-167481 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ForI-PMP Chains: A, B
Molecule details ›
Chains: A, B
Length: 424 amino acids
Theoretical weight: 44.56 KDa
Source organism: Streptomyces kaniharaensis
Expression system: Escherichia coli BL21(DE3)

Ligands and Environments

2 bound ligands:
Ligand PMP 2 x PMP
Ligand SO4 5 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P212121
Unit cell:
a: 58.264Å b: 125.828Å c: 142.747Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.169 0.167 0.192
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Biosynthesis of C-nucleoside antibiotics in actinobacteria: recent advances and future developments.
Zhang et al. (2022)
3 other articles