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 100% 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 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 Escherichia coli

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

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

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