› 1hyf

X-ray diffraction
1.7Å resolution

RIBONUCLEASE T1 V16A MUTANT IN COMPLEX WITH SR2+

Released:
DOI: 10.2210/pdb1hyf/pdb
PDB entry 1hyf coloured by chain, front view.
PDB entry 1hyf coloured by chain, side view.
PDB entry 1hyf coloured by chain, top view.
Source organism: Aspergillus oryzae
Primary publication:
The contribution of metal ions to the conformational stability of ribonuclease T1: crystal versus solution.
Deswarte J, De Vos S, Langhorst U, Steyaert J, Loris R
Eur J Biochem 268 3993-4000 (2001)
PMID: 11453993

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 Chain: A
Molecule details ›
Chain: A
Length: 104 amino acids
Theoretical weight: 11.07 KDa
Source organism: Aspergillus oryzae
Expression system: Escherichia coli
UniProt:
  • Canonical: P00651 (Residues: 27-130; Coverage: 100%)
Gene names: AO090011000118, rntA
Structure domains: Microbial ribonucleases

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P212121
Unit cell:
a: 40.445Å b: 47.166Å c: 50.093Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.188 0.203
Expression system: Escherichia coli

Quick links

Citations

4 citation in other articles

Crystal and solution structure, stability and post-translational modifications of collapsin response mediator protein 2.
Majava et al. (2008)
3 more

1 mention without citation

Structure of a highly acidic β-lactamase from the moderate halophile Chromohalobacter sp. 560 and the discovery of a Cs(+)-selective binding site.
Arai et al. (2015)