› 1pkx

X-ray diffraction
1.9Å resolution

Crystal Structure of human ATIC in complex with XMP

Released:
DOI: 10.2210/pdb1pkx/pdb
PDB entry 1pkx coloured by chain, front view.
PDB entry 1pkx coloured by chain, side view.
PDB entry 1pkx coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural insights into the human and avian IMP cyclohydrolase mechanism via crystal structures with the bound XMP inhibitor.
Wolan DW, Cheong CG, Greasley SE, Wilson IA
Biochemistry 43 1171-83 (2004)
PMID: 14756553

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

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

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: P21
Unit cell:
a: 77.52Å b: 93.56Å c: 179.88Å
α: 90° β: 91.09° γ: 90°
R-values:
R R work R free
0.211 0.211 0.249
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Structural biology of the purine biosynthetic pathway.
Zhang et al. (2008)
14 other articles

5 mentions without citation

Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli.
Zhang et al. (2009)
4 more