› 1s3y

X-ray diffraction
2.25Å resolution

Structure Determination of Tetrahydroquinazoline Antifolates in Complex with Human and Pneumocystis carinii Dihydrofolate Reductase: Correlations of Enzyme Selectivity and Stereochemistry

Released:
DOI: 10.2210/pdb1s3y/pdb
PDB entry 1s3y coloured by chain, front view.
PDB entry 1s3y coloured by chain, side view.
PDB entry 1s3y coloured by chain, top view.
Source organism: Pneumocystis carinii
Primary publication:
Structure determination of tetrahydroquinazoline antifolates in complex with human and Pneumocystis carinii dihydrofolate reductase: correlations between enzyme selectivity and stereochemistry.
Cody V, Luft JR, Pangborn W, Gangjee A, Queener SF
Acta Crystallogr D Biol Crystallogr 60 646-55 (2004)
PMID: 15039552

Function and Biology Details

Reaction catalysed: 
5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + NADPH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147657 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydrofolate reductase Chain: A
Molecule details ›
Chain: A
Length: 206 amino acids
Theoretical weight: 23.92 KDa
Source organism: Pneumocystis carinii
Expression system: Escherichia coli
UniProt:
  • Canonical: P16184 (Residues: 1-206; Coverage: 100%)
Sequence domains: Dihydrofolate reductase
Structure domains: Dihydrofolate Reductase, subunit A

Ligands and Environments


Cofactor: Ligand NAP 1 x NAP
1 bound ligand:
Ligand TQT 1 x TQT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21
Unit cell:
a: 37.359Å b: 43.286Å c: 61.397Å
α: 90° β: 94.65° γ: 90°
R-values:
R R work R free
0.289 0.233 0.289
Expression system: Escherichia coli

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Citations

1 review citation

The Art of Compiling Protein Binding Site Ensembles.
Bietz et al. (2016)
11 other articles

1 mention without citation

Built-in loops allow versatility in domain-domain interactions: lessons from self-interacting domains.
Akiva et al. (2008)