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X-ray diffraction
2.2Å resolution

X-RAY STRUCTURE OF A BETA-CARBONIC ANHYDRASE FROM THE RED ALGA, PORPHYRIDIUM PURPUREUM R-1

Released:
DOI: 10.2210/pdb1ddz/pdb
PDB entry 1ddz coloured by chain, front view.
PDB entry 1ddz coloured by chain, side view.
PDB entry 1ddz coloured by chain, top view.
Source organism: Porphyridium purpureum
Primary publication:
X-ray structure of beta-carbonic anhydrase from the red alga, Porphyridium purpureum, reveals a novel catalytic site for CO(2) hydration.
Mitsuhashi S, Mizushima T, Yamashita E, Yamamoto M, Kumasaka T, Moriyama H, Ueki T, Miyachi S, Tsukihara T
J Biol Chem 275 5521-6 (2000)
PMID: 10681531

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-174979 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
carbonic anhydrase Chains: A, B
Molecule details ›
Chains: A, B
Length: 496 amino acids
Theoretical weight: 54.99 KDa
Source organism: Porphyridium purpureum
Expression system: Escherichia coli
UniProt:
  • Canonical: Q43060 (Residues: 76-571; Coverage: 87%)
Gene names: gtPCA1, pca1
Sequence domains: Carbonic anhydrase
Structure domains: Carbonic anhydrase

Ligands and Environments

1 bound ligand:
Ligand ZN 4 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL45XU
Spacegroup: P21
Unit cell:
a: 63.5Å b: 112.8Å c: 73.2Å
α: 90° β: 103.6° γ: 90°
R-values:
R R work R free
0.208 0.208 0.274
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Carbonic anhydrase inhibitors.
Supuran et al. (2003)
8 more

8 mentions without citation

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