› 5et4

X-ray diffraction
2.1Å resolution

Structure of RNase A-K7H/R10H in complex with 3'-CMP

Released:
DOI: 10.2210/pdb5et4/pdb
PDB entry 5et4 coloured by chain, front view.
PDB entry 5et4 coloured by chain, side view.
PDB entry 5et4 coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Characterization of an RNase with two catalytic centers. Human RNase6 catalytic and phosphate-binding site arrangement favors the endonuclease cleavage of polymeric substrates.
Prats-Ejarque G, Blanco JA, Salazar VA, Nogués VM, Moussaoui M, Boix E
Biochim Biophys Acta Gen Subj 1863 105-117 (2019)
PMID: 30287244

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

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158407 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribonuclease pancreatic Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 124 amino acids
Theoretical weight: 13.7 KDa
Source organism: Bos taurus
Expression system: Escherichia coli BL21
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 C3P 4 x C3P
Ligand MPD 1 x MPD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: C2
Unit cell:
a: 160.366Å b: 32.281Å c: 106.963Å
α: 90° β: 125.71° γ: 90°
R-values:
R R work R free
0.228 0.224 0.321
Expression system: Escherichia coli BL21

Quick links

Citations

4 review citations

Primer design for quantitative real-time PCR for the emerging Coronavirus SARS-CoV-2.
Li et al. (2020)
3 more

1 mention without citation

The first crystal structure of human RNase 6 reveals a novel substrate-binding and cleavage site arrangement.
Prats-Ejarque et al. (2016)