› 4xix

X-ray diffraction
2.7Å resolution

Carbonic anhydrase Cah3 from Chlamydomonas reinhardtii in complex with phosphate.

Released:
DOI: 10.2210/pdb4xix/pdb
PDB entry 4xix coloured by chain, front view.
PDB entry 4xix coloured by chain, side view.
PDB entry 4xix coloured by chain, top view.
Source organism: Chlamydomonas reinhardtii
Primary publication:
Crystal structure and functional characterization of photosystem II-associated carbonic anhydrase CAH3 in Chlamydomonas reinhardtii.
Benlloch R, Shevela D, Hainzl T, Grundström C, Shutova T, Messinger J, Samuelsson G, Sauer-Eriksson AE
Plant Physiol 167 950-62 (2015)
PMID: 25617045

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-174459 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carbonic anhydrase Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 239 amino acids
Theoretical weight: 26.2 KDa
Source organism: Chlamydomonas reinhardtii
Expression system: Escherichia coli
UniProt:
  • Canonical: Q39588 (Residues: 73-310; Coverage: 77%)
Gene names: CAH3, CHLRE_09g415700v5
Sequence domains: Eukaryotic-type carbonic anhydrase
Structure domains: Alpha carbonic anhydrase

Ligands and Environments

2 bound ligands:
Ligand ZN 8 x ZN
Ligand 2HP 24 x 2HP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P3221
Unit cell:
a: 138.957Å b: 138.957Å c: 202.807Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.16 0.156 0.23
Expression system: Escherichia coli

Quick links

Citations

4 review citations

An Update on the Metabolic Roles of Carbonic Anhydrases in the Model Alga Chlamydomonas reinhardtii.
Aspatwar et al. (2018)
3 more

1 mention without citation

Proteins analysed as virtual knots.
Alexander et al. (2017)