› 1pl0

X-ray diffraction
2.6Å resolution

Crystal structure of human ATIC in complex with folate-based inhibitor, BW2315U89UC

Released:
DOI: 10.2210/pdb1pl0/pdb
PDB entry 1pl0 coloured by chain, front view.
PDB entry 1pl0 coloured by chain, side view.
PDB entry 1pl0 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structures of human bifunctional enzyme aminoimidazole-4-carboxamide ribonucleotide transformylase/IMP cyclohydrolase in complex with potent sulfonyl-containing antifolates.
Cheong CG, Wolan DW, Greasley SE, Horton PA, Beardsley GP, Wilson IA
J Biol Chem 279 18034-45 (2004)
PMID: 14966129

Function and Biology Details

Reactions catalysed: 
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide = tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
IMP + H(2)O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152108 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional purine biosynthesis protein ATIC Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 592 amino acids
Theoretical weight: 64.69 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P31939 (Residues: 1-592; Coverage: 100%)
Gene names: ATIC, OK/SW-cl.86, PURH
Sequence domains:
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand K 4 x K
Ligand XMP 2 x XMP
Ligand AMZ 3 x AMZ
Ligand BW2 2 x BW2
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P21
Unit cell:
a: 77.12Å b: 92.97Å c: 178.49Å
α: 90° β: 91.19° γ: 90°
R-values:
R R work R free
0.213 0.213 0.275
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Structural biology of the purine biosynthetic pathway.
Zhang et al. (2008)
3 more

2 mentions without citation

Discovery of 5-substituted pyrrolo[2,3-d]pyrimidine antifolates as dual-acting inhibitors of glycinamide ribonucleotide formyltransferase and 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase in de novo purine nucleotide biosynthesis: implications of inhibiting 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase to ampk activation and antitumor activity.
Mitchell-Ryan et al. (2013)
1 more