4cmi

X-ray diffraction
1.9Å resolution

Crystal structure of pteridine reductase 1 (PTR1) from Trypanosoma brucei in ternary complex with cofactor and inhibitor

Released:

Function and Biology Details

Reaction catalysed:
5,6,7,8-tetrahydrobiopterin + 2 NADP(+) = biopterin + 2 NADPH
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-522284 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Pteridine reductase Chains: A, D
Molecule details ›
Chains: A, D
Length: 288 amino acids
Theoretical weight: 30.69 KDa
Source organism: Trypanosoma brucei brucei
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O76290 (Residues: 1-268; Coverage: 100%)
Gene name: PTR1
Sequence domains: Enoyl-(Acyl carrier protein) reductase
Structure domains: NAD(P)-binding Rossmann-like Domain
Pteridine reductase Chains: B, C
Molecule details ›
Chains: B, C
Length: 288 amino acids
Theoretical weight: 30.67 KDa
Source organism: Trypanosoma brucei brucei
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O76290 (Residues: 1-268; Coverage: 100%)
Gene name: PTR1
Sequence domains: Enoyl-(Acyl carrier protein) reductase
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments


Cofactor: Ligand NAP 4 x NAP
2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P21
Unit cell:
a: 74.462Å b: 90.258Å c: 82.086Å
α: 90° β: 115.59° γ: 90°
R-values:
R R work R free
0.163 0.16 0.21
Expression system: Escherichia coli BL21(DE3)