› 1trp

X-ray diffraction
2.4Å resolution

X-RAY CRYSTALLOGRAPHIC AND CALORIMERIC STUDIES OF THE EFFECTS OF THE MUTATION TRP 59 TYR IN RIBONUCLEASE T1

Released:
DOI: 10.2210/pdb1trp/pdb
PDB entry 1trp coloured by chain, front view.
PDB entry 1trp coloured by chain, side view.
PDB entry 1trp coloured by chain, top view.
Source organism: Aspergillus oryzae
Primary publication:
X-ray crystallographic and calorimetric studies of the effects of the mutation Trp59-->Tyr in ribonuclease T1.
Schubert WD, Schluckebier G, Backmann J, Granzin J, Kisker C, Choe HW, Hahn U, Pfeil W, Saenger W
Eur J Biochem 220 527-34 (1994)
PMID: 8125111

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:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132808 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Guanyl-specific ribonuclease T1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 104 amino acids
Theoretical weight: 11.09 KDa
Source organism: Aspergillus oryzae
Expression system: Not provided
UniProt:
  • Canonical: P00651 (Residues: 27-130; Coverage: 100%)
Gene names: AO090011000118, rntA
Structure domains: Microbial ribonucleases

Ligands and Environments

2 bound ligands:
Ligand CA 2 x CA
Ligand 2GP 2 x 2GP
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 49.15Å b: 48.15Å c: 40.15Å
α: 90° β: 90.35° γ: 90°
R-values:
R R work R free
0.16 not available not available
Expression system: Not provided

Quick links

Citations

6 citation in other articles

Effect of surface hydrophobicity distribution on retention of ribonucleases in hydrophobic interaction chromatography.
Mahn et al. (2004)
5 more

1 mention without citation

Structural insights into the prereaction state of pyruvate decarboxylase from Zymomonas mobilis .
Pei et al. (2010)