› 6enp

X-ray diffraction
1.04Å resolution

Atomic resolution structure of human RNase 6 in the presence of phosphate anions in P21 space group.

Released:
DOI: 10.2210/pdb6enp/pdb
PDB entry 6enp coloured by chain, front view.
PDB entry 6enp coloured by chain, side view.
PDB entry 6enp coloured by chain, top view.
Source organism: Homo sapiens
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

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-187981 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribonuclease K6 Chain: A
Molecule details ›
Chain: A
Length: 128 amino acids
Theoretical weight: 14.81 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q93091 (Residues: 24-150; Coverage: 100%)
Gene names: RNASE6, RNS6
Sequence domains: Pancreatic ribonuclease
Structure domains: Ribonuclease A-like domain

Ligands and Environments

4 bound ligands:
Ligand PO4 3 x PO4
Ligand ZN 1 x ZN
Ligand NA 3 x NA
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALBA BEAMLINE XALOC
Spacegroup: P212121
Unit cell:
a: 27.734Å b: 38.557Å c: 98.965Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.123 0.122 0.145
Expression system: Escherichia coli BL21(DE3)

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Citations

4 review citations

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