› 3dl5

X-ray diffraction
2.74Å resolution

Crystal Structure of the A287F Active Site Mutant of TS-DHFR from Cryptosporidium hominis

Released:
DOI: 10.2210/pdb3dl5/pdb
PDB entry 3dl5 coloured by chain, front view.
PDB entry 3dl5 coloured by chain, side view.
PDB entry 3dl5 coloured by chain, top view.
Source organism: Cryptosporidium hominis
Primary publication:
Explaining an unusually fast parasitic enzyme: folate tail-binding residues dictate substrate positioning and catalysis in Cryptosporidium hominis thymidylate synthase.
Martucci WE, Vargo MA, Anderson KS
Biochemistry 47 8902-11 (2008)
PMID: 18672899

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-163487 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydrofolate reductase, DHFR Chains: A, B, C, D, E
Molecule details ›
Chains: A, B, C, D, E
Length: 521 amino acids
Theoretical weight: 60.34 KDa
Source organism: Cryptosporidium hominis
Expression system: Escherichia coli BL21(DE3)
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand UMP 5 x UMP
Ligand CB3 5 x CB3
Ligand DHF 5 x DHF
Ligand NDP 5 x NDP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: C2
Unit cell:
a: 214.807Å b: 116.542Å c: 219.212Å
α: 90° β: 95.21° γ: 90°
R-values:
R R work R free
0.214 0.214 0.245
Expression system: Escherichia coli BL21(DE3)

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Citations

1 review citation

Cryptosporidium: genomic and biochemical features.
Rider et al. (2010)
6 other articles

2 mentions without citation

Human-specific evolution and adaptation led to major qualitative differences in the variable receptors of human and chimpanzee natural killer cells.
Abi-Rached et al. (2010)
1 more