› 1i6p

X-ray diffraction
2Å resolution

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

Released:
DOI: 10.2210/pdb1i6p/pdb
PDB entry 1i6p coloured by chain, front view.
PDB entry 1i6p coloured by chain, side view.
PDB entry 1i6p 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 Chain: A
Molecule details ›
Chain: A
Length: 220 amino acids
Theoretical weight: 25.13 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 1 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P42212
Unit cell:
a: 68.535Å b: 68.535Å c: 85.877Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 0.176 0.202
Expression system: Escherichia coli BL21

Quick links

Citations

12 review citations

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

12 mentions without citation

Crystal structure of E. coli beta-carbonic anhydrase, an enzyme with an unusual pH-dependent activity.
Cronk et al. (2001)
11 more