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Crystal structure of the Y200A mutant of gamma carbonic anhydrase from Methanosarcina thermophila

The structure was published by Domsic, J.F., Robbins, A.H., and McKenna, R., in in a paper entitled "Crystal structure of the Y200A mutant of Methanosarcina thermophila" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.801 Å and deposited in 2010.

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

The PDB entry contains the structure of Carbonic anhydrase. This molecule has the UniProt identifier P40881 (CAH_METTE)search. The sample contained 213 residues which is 100% of the natural sequence. Out of 213 residues 205 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 homotrimers.

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 P40881 (35-247) (CAH_METTE)search Methanosarcina thermophilasearch 100% 213 96%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P40881 (35 - 247) Carbonic anhydrase Methanosarcina thermophila

Chain Sequence family (Pfam)
A (P40881) PF00132: Bacterial transferase hexapeptide (six repeats)search, PF14602: Hexapeptide repeat of succinyl-transferasesearch

Chain ID Molecular function (GO) Biological process (GO)
A (P40881) lyase activitysearch carbonate dehydratase activitysearch metal ion bindingsearch metabolic processsearch

Chain InterPro annotation
A Bacterial transferase hexapeptide repeatsearch Trimeric LpxA-likesearch