1b9l

X-ray diffraction
2.9Å resolution

7,8-DIHYDRONEOPTERIN TRIPHOSPHATE EPIMERASE

Released:

Function and Biology Details

Reaction catalysed:
7,8-dihydroneopterin 3'-triphosphate = 7,8-dihydromonapterin 3'-triphosphate
Biochemical function:
Cellular component:

Structure analysis Details

Assemblies composition:
homo octamer
homo tetramer (preferred)
PDBe Complex ID:
PDB-CPX-142232 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydroneopterin triphosphate 2'-epimerase Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 120 amino acids
Theoretical weight: 14.1 KDa
Source organism: Escherichia coli
UniProt:
  • Canonical: P0AC19 (Residues: 1-120; Coverage: 100%)
Gene names: JW2300, b2303, folX
Sequence domains: Dihydroneopterin aldolase
Structure domains: GTP Cyclohydrolase I, domain 2

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P41
Unit cell:
a: 69.68Å b: 69.68Å c: 239.72Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.188 0.259