3ucm Summary


Coccomyxa beta-carbonic anhydrase in complex with thiocyanate

The structure was published by Huang, S., Hainzl, T., Grundstrom, C., Forsman, C., Samuelsson, G., and Sauer-Eriksson, A.E., in 2011 in a paper entitled "Structural studies of [beta]-carbonic anhydrase from the green alga Coccomyxa: inhibitor complexes with anions and acetazolamide." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.513 Å and deposited in 2011.

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

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

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 Q96554 (1-227) (Q96554_9CHLO)search Coccomyxa sp. PAsearch 100% 227 97%
B Carbonic anhydrase Q96554 (1-227) (Q96554_9CHLO)search Coccomyxa sp. PAsearch 100% 227 97%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q96554 (1 - 227) Carbonic anhydrase Coccomyxa sp. PA

Chain Structural classification (CATH) Sequence family (Pfam)
A, B (Q96554) Beta-carbonic Anhydrase; Chain Asearch PF00484: Carbonic anhydrasesearch

Chain ID Biological process (GO) Molecular function (GO)
A, B (Q96554) metabolic processsearch carbon utilizationsearch zinc ion bindingsearch carbonate dehydratase activitysearch lyase activitysearch metal ion bindingsearch

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