› 3di9

X-ray diffraction
2Å resolution

Crystal structure of bovine pancreatic ribonuclease A variant (I81A)

Released:
DOI: 10.2210/pdb3di9/pdb
PDB entry 3di9 coloured by chain, front view.
PDB entry 3di9 coloured by chain, side view.
PDB entry 3di9 coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
X-ray crystallographic studies of RNase A variants engineered at the most destabilizing positions of the main hydrophobic core: further insight into protein stability.
Kurpiewska K, Font J, Ribó M, Vilanova M, Lewiński K
Proteins 77 658-69 (2009)
PMID: 19544568

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 analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
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: 13.67 KDa
Source organism: Bos taurus
Expression system: Escherichia coli BL21(DE3)
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

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

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR590
Spacegroup: P3221
Unit cell:
a: 63.982Å b: 63.982Å c: 63.716Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.198 0.198 0.243
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 citation in other articles

Simultaneous single-structure and bundle representation of protein NMR structures in torsion angle space.
Gottstein et al. (2012)
4 more

1 mention without citation

Sparse estimation for structural variability.
Hosur et al. (2011)