› 1ekj

X-ray diffraction
1.93Å resolution

THE X-RAY CRYSTALLOGRAPHIC STRUCTURE OF BETA CARBONIC ANHYDRASE FROM THE C3 DICOT PISUM SATIVUM

Released:
DOI: 10.2210/pdb1ekj/pdb
PDB entry 1ekj coloured by chain, front view.
PDB entry 1ekj coloured by chain, side view.
PDB entry 1ekj coloured by chain, top view.
Source organism: Pisum sativum
Primary publication:
The active site architecture of Pisum sativum beta-carbonic anhydrase is a mirror image of that of alpha-carbonic anhydrases.
Kimber MS, Pai EF
EMBO J 19 1407-18 (2000)
PMID: 10747009

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 octamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147864 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carbonic anhydrase, 25 kDa isoform Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 221 amino acids
Theoretical weight: 23.97 KDa
Source organism: Pisum sativum
UniProt:
  • Canonical: P17067 (Residues: 108-328; Coverage: 67%)
Sequence domains: Carbonic anhydrase
Structure domains: Carbonic anhydrase

Ligands and Environments

7 bound ligands:
Ligand ACT 9 x ACT
Ligand AZI 4 x AZI
Ligand ZN 8 x ZN
Ligand CL 8 x CL
Ligand EDO 4 x EDO
Ligand CU 4 x CU
Ligand CIT 1 x CIT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS
Spacegroup: C222
Unit cell:
a: 136.909Å b: 143.318Å c: 202.135Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.229 0.229 0.25

Quick links

Citations

27 review citations

Carbonic anhydrases as targets for medicinal chemistry.
Supuran et al. (2007)
26 more

18 mentions without citation

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