3eyx Summary

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Crystal structure of Carbonic Anhydrase Nce103 from Saccharomyces cerevisiae

The structure was published by Teng, Y.B., Jiang, Y.L., He, Y.X., et al., Lian, F.M., Chen, Y., and Zhou, C.Z., in 2009 in a paper entitled "Structural insights into the substrate tunnel of Saccharomyces cerevisiae carbonic anhydrase Nce103." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.04 Å and deposited in 2008.

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 homodimers.

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 P53615 (14-221) (CAN_YEAST)search Saccharomyces cerevisiae S288csearch 94% 216 91%
B Carbonic anhydrase P53615 (14-221) (CAN_YEAST)search Saccharomyces cerevisiae S288csearch 94% 216 91%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P53615 (14 - 221) Carbonic anhydrase Saccharomyces cerevisiae

Chain Sequence family (Pfam)
A, B (P53615) PF00484: Carbonic anhydrasesearch

Chain ID Biological process (GO) Molecular function (GO) Cellular component (GO)
A, B (P53615) metabolic processsearch cellular response to oxidative stresssearch cellular response to carbon dioxidesearch lyase activitysearch carbonate dehydratase activitysearch metal ion bindingsearch nucleussearch cytoplasmsearch mitochondrial intermembrane spacesearch mitochondrionsearch

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