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PDBe Entry: 1i6o view

CRYSTAL STRUCTURE OF E. COLI BETA CARBONIC ANHYDRASE (ECCA)
Summary
Header LYASEsearch
Method X-RAY DIFFRACTION
Experiment Resolution: 2.2 Å, R-factor: 21.2%, Free R-factor: 24.3%, Spacegroup: P 43 2 2
Released 09/05/2001, deposition: 02/03/2001, last revision: 24/02/2009
Authors Cronk, J.D.search; Endrizzi, J.A.search; Cronk, M.R.search; O'Neill, J.W.search; Zhang, K.Y.J.search
Primary citation Crystal structure of E. coli beta-carbonic anhydrase, an enzyme with an unusual pH-dependent activity.
PROTEIN SCI.search vol:10, pag:911-922 (2001) [PubMed ID 11316870 ]search
Keywords carbonic anhydrasesearch, metalloenzymesearch, zinc coordinationsearch, pH-dependent activitysearch, MAD phasingsearch, crystal structuresearch, LYASEsearch
EC 4.2.1.1 ExPASy BRENDA search (A B)
Organism Escherichia coli 562search(A B)
UniProt Carbonic anhydrase 2 (EC 4.2.1.1) (Carbonate dehydratase 2) P61517search (A B)
Solvent A, B
Related entries 1i6p
Polymers
Id Name Type UniProt Residues Observed
A, B CARBONIC ANHYDRASE Protein P61517 (CAN_ECOLI)search
220 97%
Heterogens
Id Name Ligands
A, B ZINC ION ZN search
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