2esf Summary

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Identification of a Novel Non-Catalytic Bicarbonate Binding Site in Eubacterial beta-Carbonic Anhydrase

The structure was published by Cronk, J.D., Rowlett, R.S., Zhang, K.Y.J., et al., Lee, J., Gareiss, P.C., and Preiss, J.R., in 2006 in a paper entitled "Identification of a Novel Noncatalytic Bicarbonate Binding Site in Eubacterial beta-Carbonic Anhydrase." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.25 Å and deposited in 2005.

The experimental data on which the structure is based was also deposited.

This PDB entry contains multiple copies of the structure of Carbonic anhydrase 2.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule most likely forms homotetramers.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A Carbonic anhydrase 2 P61517 (1-220) (CAN_ECOLI)search Escherichia coli K-12search 100% 220 97%
B Carbonic anhydrase 2 P61517 (1-220) (CAN_ECOLI)search Escherichia coli K-12search 100% 220 97%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P61517 (1 - 220) Carbonic anhydrase 2 Escherichia coli

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B (P61517) beta-carbonic anhydrase, cabsearch Beta-carbonic Anhydrase; Chain Asearch PF00484: Carbonic anhydrasesearch

Chain ID Molecular function (GO) Biological process (GO) Cellular component (GO)
A, B (P61517) zinc ion bindingsearch carbonate dehydratase activitysearch metal ion bindingsearch lyase activitysearch carbon utilizationsearch metabolic processsearch cytosolsearch

Chain InterPro annotation
A, B Carbonic anhydrasesearch Carbonic anhydrase, prokaryotic-like, conserved sitesearch