› 3o1k

X-ray diffraction
1.95Å resolution

Crystal structure of putative dihydroneopterin aldolase (FolB) from Vibrio cholerae O1 biovar El Tor str. N16961

Released:
DOI: 10.2210/pdb3o1k/pdb
PDB entry 3o1k coloured by chain, front view.
PDB entry 3o1k coloured by chain, side view.
PDB entry 3o1k coloured by chain, top view.
Source organism: Vibrio cholerae O1 biovar El Tor str. N16961
Entry authors: Nocek B, Zhou M, Papazisi L, Anderson W, 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:
Sequence domains:

Structure analysis Details

Assemblies composition:
homo octamer
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192115 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
7,8-dihydroneopterin aldolase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 132 amino acids
Theoretical weight: 14.87 KDa
Source organism: Vibrio cholerae O1 biovar El Tor str. N16961
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9KUJ6 (Residues: 1-129; Coverage: 100%)
Gene name: VC_0524
Sequence domains: Dihydroneopterin aldolase
Structure domains: GTP Cyclohydrolase I, domain 2

Ligands and Environments

1 bound ligand:
Ligand EDO 1 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: C2221
Unit cell:
a: 95.098Å b: 101.734Å c: 116.397Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.194 0.246
Expression system: Escherichia coli BL21(DE3)

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