3efi Summary

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Carbonic anhydrase activators: Kinetic and X-ray crystallographic study for the interaction of d- and l-tryptophan with the mammalian isoforms I-XIV

The structure was published by Temperini, C., Innocenti, A., Scozzafava, A., and Supuran, C.T., in 2008 in a paper entitled "Carbonic anhydrase activators: kinetic and X-ray crystallographic study for the interaction of D- and L-tryptophan with the mammalian isoforms I-XIV" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.75 Å and deposited in 2008.

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

The PDB entry contains the structure of Carbonic anhydrase 2. This molecule has the UniProt identifier P00918 (CAH2_HUMAN)search. The sample contained 260 residues which is < 90% of the natural sequence. Out of 260 residues 256 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 is most likely monomeric.

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 Not available
Synthetic Not available 260 98%


Chain Structural classification (SCOP) Structural classification (CATH)
A Carbonic anhydrasesearch Carbonic Anhydrase IIsearch

Chain ID Biological process (GO) Molecular function (GO)
A () one-carbon metabolic processsearch carbonate dehydratase activitysearch zinc ion bindingsearch

Chain InterPro annotation
A Alpha carbonic anhydrasesearch Carbonic anhydrase, alpha-class, conserved sitesearch Carbonic anhydrase 2search Carbonic anhydrase, alpha-classsearch