› 6gcl

X-ray diffraction
1.95Å resolution

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-131225 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Pteridine reductase Chains: A, B, D
Molecule details ›
Chains: A, B, D
Length: 288 amino acids
Theoretical weight: 30.67 KDa
Source organism: Trypanosoma brucei brucei
Expression system: Escherichia coli
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 Chain: C
Molecule details ›
Chain: C
Length: 288 amino acids
Theoretical weight: 30.72 KDa
Source organism: Trypanosoma brucei brucei
Expression system: Escherichia coli
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

2 bound ligands:
Ligand NAP 4 x NAP
Ligand EUE 4 x EUE
1 modified residue:
Ligand OCS 1 x OCS

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P21
Unit cell:
a: 74.87Å b: 91.06Å c: 83.08Å
α: 90° β: 115.92° γ: 90°
R-values:
R R work R free
0.191 0.189 0.243
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Structure and dynamics of pteridine reductase 1: the key phenomena relevant to enzyme function and drug design.
Panecka-Hofman et al. (2023)
7 other articles