› 1rj5

X-ray diffraction
2.81Å resolution

Crystal Structure of the Extracellular Domain of Murine Carbonic Anhydrase XIV

Released:
DOI: 10.2210/pdb1rj5/pdb
PDB entry 1rj5 coloured by chain, front view.
PDB entry 1rj5 coloured by chain, side view.
PDB entry 1rj5 coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Expression, assay, and structure of the extracellular domain of murine carbonic anhydrase XIV: implications for selective inhibition of membrane-associated isozymes.
Whittington DA, Grubb JH, Waheed A, Shah GN, Sly WS, Christianson DW
J Biol Chem 279 7223-8 (2004)
PMID: 14660577

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-194412 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
Carbonic anhydrase 14 Chains: A, B
Molecule details ›
Chains: A, B
Length: 261 amino acids
Theoretical weight: 29.33 KDa
Source organism: Mus musculus
Expression system: Chlorocebus aethiops
UniProt:
  • Canonical: Q9WVT6 (Residues: 18-278; Coverage: 81%)
Gene names: Ca14, Car14, Catm
Sequence domains: Eukaryotic-type carbonic anhydrase
Structure domains: Alpha carbonic anhydrase

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, BMA
Carbohydrate polymer
3 bound ligands:
Ligand ZN 2 x ZN
Ligand CL 1 x CL
Ligand ACY 2 x ACY
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P21
Unit cell:
a: 59Å b: 75.6Å c: 73.2Å
α: 90° β: 98.9° γ: 90°
R-values:
R R work R free
0.234 0.234 0.274
Expression system: Chlorocebus aethiops

Quick links

Citations

16 review citations

Structure-based drug discovery of carbonic anhydrase inhibitors.
Supuran CT. (2012)
15 more

5 mentions without citation

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