› 3bn1

X-ray diffraction
1.8Å resolution

Crystal structure of GDP-perosamine synthase

Released:
DOI: 10.2210/pdb3bn1/pdb
PDB entry 3bn1 coloured by chain, front view.
PDB entry 3bn1 coloured by chain, side view.
PDB entry 3bn1 coloured by chain, top view.
Source organism: Caulobacter vibrioides CB15
Primary publication:
GDP-perosamine synthase: structural analysis and production of a novel trideoxysugar.
Cook PD, Holden HM
Biochemistry 47 2833-40 (2008)
PMID: 18247575

Function and Biology Details

Reaction catalysed: 
GDP-4-amino-4,6-dideoxy-alpha-D-mannose + 2-oxoglutarate = GDP-4-dehydro-6-deoxy-alpha-D-mannose + L-glutamate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-189505 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
GDP-perosamine synthase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 373 amino acids
Theoretical weight: 41.07 KDa
Source organism: Caulobacter vibrioides CB15
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9A9H3 (Residues: 2-371; Coverage: 100%)
Gene names: CC_1012, per
Sequence domains: DegT/DnrJ/EryC1/StrS aminotransferase family
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand ACT 3 x ACT
Ligand NA 1 x NA
Ligand AKG 1 x AKG
1 modified residue:
Ligand LLP 4 x LLP

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21
Unit cell:
a: 50.271Å b: 152.933Å c: 105.726Å
α: 90° β: 102.09° γ: 90°
R-values:
R R work R free
0.179 0.176 0.253
Expression system: Escherichia coli

Quick links

Citations

4 review citations

The structural biology of enzymes involved in natural product glycosylation.
Singh et al. (2012)
3 more

2 mentions without citation

Cytomegalovirus Genetic Diversity Following Primary Infection.
Ross et al. (2020)
1 more