› 2rat

X-ray diffraction
1.5Å resolution

EFFECTS OF TEMPERATURE ON PROTEIN STRUCTURE AND DYNAMICS: X-RAY CRYSTALLOGRAPHIC STUDIES OF THE PROTEIN RIBONUCLEASE-A AT NINE DIFFERENT TEMPERATURES FROM 98 TO 320 K

Released:
DOI: 10.2210/pdb2rat/pdb
PDB entry 2rat coloured by chain, front view.
PDB entry 2rat coloured by chain, side view.
PDB entry 2rat coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Effects of temperature on protein structure and dynamics: X-ray crystallographic studies of the protein ribonuclease-A at nine different temperatures from 98 to 320 K.
Tilton RF, Dewan JC, Petsko GA
Biochemistry 31 2469-81 (1992)
PMID: 1547232

Function and Biology Details

Reaction catalysed: 
(1a) an (RNA) containing cytidine = an (RNA)-3'-cytidine-2',3'-cyclophosphate + a 5'-hydroxy-ribonucleotide-3'-(RNA)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158390 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribonuclease pancreatic Chain: A
Molecule details ›
Chain: A
Length: 124 amino acids
Theoretical weight: 13.71 KDa
Source organism: Bos taurus
Expression system: Not provided
UniProt:
  • Canonical: P61823 (Residues: 27-150; Coverage: 100%)
Gene names: RNASE1, RNS1
Sequence domains: Pancreatic ribonuclease
Structure domains: Ribonuclease A-like domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 29.48Å b: 38.12Å c: 53.24Å
α: 90° β: 106.01° γ: 90°
R-values:
R R work R free
0.148 not available not available
Expression system: Not provided

Quick links

Citations

28 review citations

Theory of protein folding: the energy landscape perspective.
Onuchic et al. (1997)
27 more

1 mention without citation

Structure of bovine pancreatic ribonuclease complexed with uridine 5'-monophosphate at 1.60 A resolution.
Larson et al. (2010)