› 2fni

X-ray diffraction
3Å resolution

Function and Biology Details

Reaction catalysed: 
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine + 2-oxoglutarate = UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-hex-4-ulose + L-glutamate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-518814 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase Chains: A, B
Molecule details ›
Chains: A, B
Length: 375 amino acids
Theoretical weight: 42.46 KDa
Source organism: Helicobacter pylori 26695
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O25130 (Residues: 1-375; Coverage: 100%)
Gene names: HP_0366, pseC
Sequence domains: DegT/DnrJ/EryC1/StrS aminotransferase family
Structure domains:

Ligands and Environments


Cofactor: Ligand PLP 2 x PLP
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P21212
Unit cell:
a: 87.4Å b: 153.3Å c: 70.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.196 0.258
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

19 review citations

Campylobacter flagella: not just for motility.
Guerry P. (2007)
18 more

2 mentions without citation

Structural Consideration of the Working Mechanism of Fold Type I Transaminases From Eubacteria: Overt and Covert Movement.
Kwon et al. (2019)
1 more