› 1mdz

X-ray diffraction
2.07Å resolution

Function and Biology Details

Reaction catalysed: 
UDP-4-amino-4-deoxy-beta-L-arabinose + 2-oxoglutarate = UDP-beta-L-threo-pentapyranos-4-ulose + L-glutamate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-187298 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UDP-4-amino-4-deoxy-L-arabinose--oxoglutarate aminotransferase Chain: A
Molecule details ›
Chain: A
Length: 393 amino acids
Theoretical weight: 42.83 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8ZNF3 (Residues: 1-385; Coverage: 100%)
Gene names: STM2297, arnB, pbgP, pbgP1, pmrH
Sequence domains: DegT/DnrJ/EryC1/StrS aminotransferase family
Structure domains:

Ligands and Environments


Cofactor: Ligand PLP 1 x PLP
1 bound ligand:
Ligand DCS 1 x DCS
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P43212
Unit cell:
a: 90.904Å b: 90.904Å c: 127.71Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.223 0.212 0.25
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Lipid A modification systems in gram-negative bacteria.
Raetz et al. (2007)
6 more

4 mentions without citation

Inhibition of the PLP-dependent enzyme serine palmitoyltransferase by cycloserine: evidence for a novel decarboxylative mechanism of inactivation.
Lowther et al. (2010)
3 more