› 4xz5

X-ray diffraction
2.6Å resolution

Structure of the thermostable alpha-Carbonic Anydrase from Thiomicrospira crunogena XCL-2 gammaproteobacterium

Released:
DOI: 10.2210/pdb4xz5/pdb
PDB entry 4xz5 coloured by chain, front view.
PDB entry 4xz5 coloured by chain, side view.
PDB entry 4xz5 coloured by chain, top view.
Source organism: Hydrogenovibrio crunogenus XCL-2
Primary publication:
Structural and biophysical characterization of the α-carbonic anhydrase from the gammaproteobacterium Thiomicrospira crunogena XCL-2: insights into engineering thermostable enzymes for CO2 sequestration.
Díaz-Torres NA, Mahon BP, Boone CD, Pinard MA, Tu C, Ng R, Agbandje-McKenna M, Silverman D, Scott K, McKenna R
Acta Crystallogr D Biol Crystallogr 71 1745-56 (2015)
PMID: 26249355

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 analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-174261 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-carbonic anhydrase domain-containing protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 233 amino acids
Theoretical weight: 26.68 KDa
Source organism: Hydrogenovibrio crunogenus XCL-2
Expression system: Escherichia coli
UniProt:
  • Canonical: Q31FD6 (Residues: 75-306; Coverage: 80%)
Gene name: Tcr_1545
Sequence domains: Eukaryotic-type carbonic anhydrase
Structure domains: Alpha carbonic anhydrase

Ligands and Environments

2 bound ligands:
Ligand ZN 4 x ZN
Ligand BCT 4 x BCT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F1
Spacegroup: C2
Unit cell:
a: 127.059Å b: 102.228Å c: 105.021Å
α: 90° β: 127.26° γ: 90°
R-values:
R R work R free
0.175 0.171 0.24
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Thermodynamic, kinetic, and structural parameterization of human carbonic anhydrase interactions toward enhanced inhibitor design.
Linkuvienė et al. (2018)
6 other articles

2 mentions without citation

Structural and biophysical characterization of the α-carbonic anhydrase from the gammaproteobacterium Thiomicrospira crunogena XCL-2: insights into engineering thermostable enzymes for CO2 sequestration.
Díaz-Torres et al. (2015)
1 more