X-ray diffraction
2.05Å resolution

QueD soaked with sepiapterin (selenomethionine substituted protein)


Function and Biology Details

Reaction catalysed:
7,8-dihydroneopterin 3'-triphosphate + H(2)O = 6-carboxy-5,6,7,8-tetrahydropterin + acetaldehyde + triphosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Entry contents:
1 distinct polypeptide molecule
6-carboxy-5,6,7,8-tetrahydropterin synthase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 121 amino acids
Theoretical weight: 13.98 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
  • Canonical: P65870 (Residues: 1-121; Coverage: 100%)
Gene names: JW2735, b2765, queD, ygcM
Sequence domains: 6-pyruvoyl tetrahydropterin synthase
Structure domains: 6-pyruvoyl tetrahydropterin synthase/QueD

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: P41212
Unit cell:
a: 111.297Å b: 111.297Å c: 126.047Å
α: 90° β: 90° γ: 90°
R R work R free
0.226 0.224 0.255
Expression system: Escherichia coli BL21(DE3)