› 1uck

X-ray diffraction
1.8Å resolution

Mutants of RNase Sa

Released:
DOI: 10.2210/pdb1uck/pdb
Model geometry
Fit model/data
Data not deposited
PDB entry 1uck coloured by chain, front view.
PDB entry 1uck coloured by chain, side view.
PDB entry 1uck coloured by chain, top view.
Source organism: Kitasatospora aureofaciens
Primary publication:
The contribution of polar group burial to protein stability is strongly context-dependent.
Takano K, Scholtz JM, Sacchettini JC, Pace CN
J Biol Chem 278 31790-5 (2003)
PMID: 12799387

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138777 (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: Escherichia coli
UniProt:
  • Canonical: P05798 (Residues: 1-96; Coverage: 100%)
Gene name: rnaSA
Sequence domains: ribonuclease
Structure domains: Microbial ribonucleases

Ligands and Environments

1 bound ligand:
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
Spacegroup: P212121
Unit cell:
a: 64.265Å b: 77.916Å c: 38.281Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.177 0.177 0.214
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Structure and energetics of the hydrogen-bonded backbone in protein folding.
Bolen et al. (2008)
5 more