1i6p Summary

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

The structure was published by Cronk, J.D., Endrizzi, J.A., Cronk, M.R., O'neill, J.W., and Zhang, K.Y., in 2001 in a paper entitled "Crystal structure of E. coli beta-carbonic anhydrase, an enzyme with an unusual pH-dependent activity." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 2001.

The experimental data on which the structure is based was not deposited.

The PDB entry contains the structure of CARBONIC ANHYDRASE. This molecule has the UniProt identifier P61517 (CAN_ECOLI)search. The sample contained 220 residues which is < 90% of the natural sequence. Out of 220 residues 214 were observed and are deposited in the PDB.

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 Not available
Escherichia colisearch Not available 220 97%


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

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