› 1keq

X-ray diffraction
1.88Å resolution

Crystal Structure of F65A/Y131C Carbonic Anhydrase V, covalently modified with 4-chloromethylimidazole

Released:
DOI: 10.2210/pdb1keq/pdb
PDB entry 1keq coloured by chain, front view.
PDB entry 1keq coloured by chain, side view.
PDB entry 1keq coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Crystal structure of F65A/Y131C-methylimidazole carbonic anhydrase V reveals architectural features of an engineered proton shuttle.
Jude KM, Wright SK, Tu C, Silverman DN, Viola RE, Christianson DW
Biochemistry 41 2485-91 (2002)
PMID: 11851394

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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 248 amino acids
Theoretical weight: 28.14 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P23589 (Residues: 53-299; Coverage: 83%)
Gene names: Ca5, Ca5a, Car5, Car5a
Sequence domains: Eukaryotic-type carbonic anhydrase
Structure domains: Alpha carbonic anhydrase

Ligands and Environments

4 bound ligands:
Ligand K 1 x K
Ligand ZN 2 x ZN
Ligand 4MZ 5 x 4MZ
Ligand ACY 3 x ACY
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12B
Spacegroup: C2
Unit cell:
a: 99.299Å b: 66.703Å c: 92.563Å
α: 90° β: 105.7° γ: 90°
R-values:
R R work R free
0.185 0.185 0.217
Expression system: Escherichia coli

Quick links

Citations

19 citation in other articles

Proton transfer in catalysis and the role of proton shuttles in carbonic anhydrase.
Mikulski et al. (2010)
18 more

4 mentions without citation

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