3e24 Summary

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H. influenzae beta-carbonic anhydrase, variant W39F

The structure was published by Rowlett, R.S., Tu, C., Lee, J., et al., Chapnick, D.A., Shah, S.H., and Gareiss, P.C., in 2009 in a paper entitled "Allosteric site variants of Haemophilus influenzae beta-carbonic anhydrase." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.301 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 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 P45148 (1-229) (CAN_HAEIN)search Haemophilus influenzae Rd KW20search 97% 229 81%
B Carbonic anhydrase 2 P45148 (1-229) (CAN_HAEIN)search Haemophilus influenzae Rd KW20search 97% 229 81%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P45148 (1 - 229) Carbonic anhydrase 2 Haemophilus influenzae

Chain Structural classification (CATH) Sequence family (Pfam)
A, B (P45148) Beta-carbonic Anhydrase; Chain Asearch PF00484: Carbonic anhydrasesearch

Chain ID Molecular function (GO) Biological process (GO) Cellular component (GO)
A, B (P45148) zinc ion bindingsearch lyase activitysearch carbonate dehydratase activitysearch metal ion bindingsearch carbon utilizationsearch metabolic processsearch cellular_componentsearch

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