› 1i6o

X-ray diffraction
2.2Å resolution

CRYSTAL STRUCTURE OF E. COLI BETA CARBONIC ANHYDRASE (ECCA)

Released:
DOI: 10.2210/pdb1i6o/pdb
PDB entry 1i6o coloured by chain, front view.
PDB entry 1i6o coloured by chain, side view.
PDB entry 1i6o coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structure of E. coli beta-carbonic anhydrase, an enzyme with an unusual pH-dependent activity.
Cronk JD, Endrizzi JA, Cronk MR, O'neill JW, Zhang KY
Protein Sci 10 911-22 (2001)
PMID: 11316870

Function and Biology Details

Reaction catalysed: 
H(2)CO(3) = CO(2) + H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158270 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carbonic anhydrase 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 220 amino acids
Theoretical weight: 25.37 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P61517 (Residues: 1-220; Coverage: 100%)
Gene names: JW0122, b0126, can, cynT2, yadF
Sequence domains: Carbonic anhydrase
Structure domains: Carbonic anhydrase

Ligands and Environments

1 bound ligand:
Ligand ZN 2 x ZN
1 modified residue:
Ligand MSE 10 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P4322
Unit cell:
a: 81.244Å b: 81.244Å c: 162.137Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.212 0.212 0.243
Expression system: Escherichia coli BL21

Quick links

Citations

11 review citations

Carbonic anhydrases: current state of the art, therapeutic applications and future prospects.
Pastorekova et al. (2004)
10 more

5 mentions without citation

Carbonic Anhydrase Inhibitors as Novel Antibacterials in the Era of Antibiotic Resistance: Where Are We Now?
Nocentini et al. (2023)
4 more