› 1gmp

X-ray diffraction
1.7Å resolution

COMPLEX OF RIBONUCLEASE FROM STREPTOMYCES AUREOFACIENS WITH 2'-GMP AT 1.7 ANGSTROMS RESOLUTION

Released:
DOI: 10.2210/pdb1gmp/pdb
PDB entry 1gmp coloured by chain, front view.
PDB entry 1gmp coloured by chain, side view.
PDB entry 1gmp coloured by chain, top view.
Source organism: Kitasatospora aureofaciens
Primary publication:
Complex of ribonuclease from Streptomyces aureofaciens with 2'-GMP at 1.7 A resolution.
Sevcik J, Hill CP, Dauter Z, Wilson KS
Acta Crystallogr D Biol Crystallogr 49 257-71 (1993)
PMID: 15299531

Function and Biology Details

Reaction catalysed: 
(1a) (RNA) containing guanosine = (RNA fragment)-3'-guanosine-2',3'-cyclophosphate + a 5'-hydroxy-ribonucleotide-3'-(RNA fragment)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138780 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Guanyl-specific ribonuclease Sa Chains: A, B
Molecule details ›
Chains: A, B
Length: 96 amino acids
Theoretical weight: 10.58 KDa
Source organism: Kitasatospora aureofaciens
Expression system: Not provided
UniProt:
  • Canonical: P05798 (Residues: 1-96; Coverage: 100%)
Gene name: rnaSA
Sequence domains: ribonuclease
Structure domains: Microbial ribonucleases

Ligands and Environments

2 bound ligands:
Ligand SO4 1 x SO4
Ligand 2GP 2 x 2GP
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 64.7Å b: 78.8Å c: 39.1Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.133 not available not available
Expression system: Not provided

Quick links

Citations

1 review citation

Ribonucleases as potential modalities in anticancer therapy.
Ardelt et al. (2009)
6 other articles

3 mentions without citation

Sequence and structural analysis of the Asp-box motif and Asp-box beta-propellers; a widespread propeller-type characteristic of the Vps10 domain family and several glycoside hydrolase families.
Quistgaard et al. (2009)
2 more