3r2e

X-ray diffraction
2.15Å resolution

Dihydroneopterin aldolase/dihydroneopterin triphosphate 2'-epimerase from Yersinia pestis.

Released:
Source organism: Yersinia pestis
Entry authors: Osipiuk J, Maltseva N, Makowska-Grzyska M, Papazisi L, Anderson WF, Joachimiak A, Center for Structural Genomics of Infectious Diseases (CSGID)

Function and Biology Details

Reaction catalysed:
7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo octamer (preferred)
PDBe Complex ID:
PDB-CPX-105469 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
7,8-dihydroneopterin aldolase Chain: A
Molecule details ›
Chain: A
Length: 143 amino acids
Theoretical weight: 16.15 KDa
Source organism: Yersinia pestis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A5P8YJX5 (Residues: 1-119; Coverage: 100%)
Gene names: YPO0648, folB
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
X-ray source: APS BEAMLINE 19-BM
Spacegroup: I422
Unit cell:
a: 71.716Å b: 71.716Å c: 107.629Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.217 0.215 0.255
Expression system: Escherichia coli BL21(DE3)