› 5uy8

X-ray diffraction
2.39Å resolution

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 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: 601 amino acids
Theoretical weight: 65.79 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P31939 (Residues: 2-592; Coverage: 100%)
Gene names: ATIC, OK/SW-cl.86, PURH
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand 8UM 4 x 8UM
Ligand AMZ 7 x AMZ
Ligand MG 4 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 31-ID
Spacegroup: P1
Unit cell:
a: 61.575Å b: 104.226Å c: 105.473Å
α: 113.16° β: 99.39° γ: 95.5°
R-values:
R R work R free
0.207 0.205 0.245
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Folic Acid Antagonists: Antimicrobial and Immunomodulating Mechanisms and Applications.
Fernández-Villa et al. (2019)
2 more

1 mention without citation

Magic angle spinning NMR structure of human cofilin-2 assembled on actin filaments reveals isoform-specific conformation and binding mode.
Kraus et al. (2022)