› 5cpv

X-ray diffraction
1.6Å resolution

RESTRAINED LEAST SQUARES REFINEMENT OF NATIVE (CALCIUM) AND CADMIUM-SUBSTITUTED CARP PARVALBUMIN USING X-RAY CRYSTALLOGRAPHIC DATA AT 1.6-ANGSTROMS RESOLUTION

Released:
DOI: 10.2210/pdb5cpv/pdb
PDB entry 5cpv coloured by chain, front view.
PDB entry 5cpv coloured by chain, side view.
PDB entry 5cpv coloured by chain, top view.
Source organism: Cyprinus carpio
Primary publication:
Restrained least squares refinement of native (calcium) and cadmium-substituted carp parvalbumin using X-ray crystallographic data at 1.6-A resolution.
Swain AL, Kretsinger RH, Amma EL
J Biol Chem 264 16620-8 (1989)
PMID: 2777802

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-135963 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Parvalbumin beta Chain: A
Molecule details ›
Chain: A
Length: 109 amino acids
Theoretical weight: 11.48 KDa
Source organism: Cyprinus carpio
Expression system: Not provided
UniProt:
  • Canonical: P02618 (Residues: 1-108; Coverage: 100%)
Sequence domains: EF-hand domain pair
Structure domains: EF-hand

Ligands and Environments

1 bound ligand:
Ligand CA 2 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2
Unit cell:
a: 28.7Å b: 60.61Å c: 54.35Å
α: 90° β: 94.6° γ: 90°
R-values:
R R work R free
0.187 not available not available
Expression system: Not provided

Quick links

Citations

4 review citations

Molecular tuning of ion binding to calcium signaling proteins.
Falke et al. (1994)
3 more

9 mentions without citation

Polarizable Force Fields for Biomolecular Simulations: Recent Advances and Applications.
Jing et al. (2019)
8 more