3i2b

X-ray diffraction
2.3Å resolution

The crystal structure of human 6 Pyruvoyl Tetrahydrobiopterin Synthase

Released:
Source organism: Homo sapiens
Entry authors: Ugochukwu E, Cocking R, Pilka E, Yue WW, Bray JE, Chaikuad A, Krojer T, Muniz J, von Delft F, Bountra C, Arrowsmith CH, Weigelt J, Edwards A, Oppermann U, Structural Genomics Consortium (SGC)

Function and Biology Details

Reaction catalysed:
7,8-dihydroneopterin 3'-triphosphate = 6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate
Cellular component:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
6-pyruvoyl tetrahydrobiopterin synthase Chains: A, B, C, D, E, F, G, H, I, J, K, L
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L
Length: 141 amino acids
Theoretical weight: 16.06 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q03393 (Residues: 7-145; Coverage: 96%)
Gene name: PTS
Sequence domains: 6-pyruvoyl tetrahydropterin synthase
Structure domains: 6-pyruvoyl tetrahydropterin synthase/QueD

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P212121
Unit cell:
a: 73.29Å b: 118.72Å c: 234.98Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.208 0.206 0.246
Expression system: Escherichia coli