› 1urt

X-ray diffraction
2.8Å resolution

MURINE CARBONIC ANHYDRASE V

Released:
DOI: 10.2210/pdb1urt/pdb
PDB entry 1urt coloured by chain, front view.
PDB entry 1urt coloured by chain, side view.
PDB entry 1urt coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Structure-based design of an intramolecular proton transfer site in murine carbonic anhydrase V.
Heck RW, Boriack-Sjodin PA, Qian M, Tu C, Christianson DW, Laipis PJ, Silverman DN
Biochemistry 35 11605-11 (1996)
PMID: 8794740

Function and Biology Details

Reaction catalysed: 
H(2)CO(3) = CO(2) + H(2)O
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150021 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carbonic anhydrase 5A, mitochondrial Chain: A
Molecule details ›
Chain: A
Length: 248 amino acids
Theoretical weight: 28.2 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P23589 (Residues: 52-299; Coverage: 83%)
Gene names: Ca5, Ca5a, Car5, Car5a
Sequence domains: Eukaryotic-type carbonic anhydrase
Structure domains: Alpha carbonic anhydrase

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2
Unit cell:
a: 101.09Å b: 67.52Å c: 48.86Å
α: 90° β: 107.6° γ: 90°
R-values:
R R work R free
0.137 0.137 0.241
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Voltage-gated proton channels and other proton transfer pathways.
Decoursey TE. (2003)
9 other articles

2 mentions without citation

Carbonic anhydrase as a model for biophysical and physical-organic studies of proteins and protein-ligand binding.
Krishnamurthy et al. (2008)
1 more