› 1h52

X-ray diffraction
2Å resolution

Binding of Phosphate and Pyrophosphate ions at the active site of human Angiogenin as revealed by X-ray Crystallography

Released:
DOI: 10.2210/pdb1h52/pdb
PDB entry 1h52 coloured by chain, front view.
PDB entry 1h52 coloured by chain, side view.
PDB entry 1h52 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Binding of phosphate and pyrophosphate ions at the active site of human angiogenin as revealed by X-ray crystallography.
Leonidas DD, Chavali GB, Jardine AM, Li S, Shapiro R, Acharya KR
Protein Sci 10 1669-76 (2001)
PMID: 11468363

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137273 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Angiogenin Chain: A
Molecule details ›
Chain: A
Length: 123 amino acids
Theoretical weight: 14.15 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P03950 (Residues: 25-147; Coverage: 100%)
Gene names: ANG, RNASE5
Sequence domains: Pancreatic ribonuclease
Structure domains: Ribonuclease A-like domain

Ligands and Environments

1 bound ligand:
Ligand POP 1 x POP
1 modified residue:
Ligand PCA 1 x PCA

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.5
Spacegroup: P21212
Unit cell:
a: 86.021Å b: 37.778Å c: 32.973Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.235 0.235 0.287
Expression system: Escherichia coli

Quick links

Citations

1 review citation

New insights into the role of angiogenin in actin polymerization.
Pyatibratov et al. (2012)
10 other articles

3 mentions without citation

A small-molecule inhibitor of the ribonucleolytic activity of human angiogenin that possesses antitumor activity.
Kao et al. (2002)
2 more