A CLOSER LOOK AT THE ACTIVE SITE OF GAMMA-CARBONIC ANHYDRASES: HIGH RESOLUTION CRYSTAL STRUCTURES OF THE CARBONIC ANHYDRASE FROM METHANOSARCINA THERMOPHILA
The structure was published by Iverson, T.M., Alber, B.E., Kisker, C., Ferry, J.G., and Rees, D.C., in 2000 in a paper entitled "A closer look at the active site of gamma-class carbonic anhydrases: high-resolution crystallographic studies of the carbonic anhydrase from Methanosarcina thermophila." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.95 Å and deposited in 1999.
The experimental data on which the structure is based was not deposited.
The PDB entry contains the structure of CARBONIC ANHYDRASE. This molecule has the UniProt identifier P40881 (CAH_METTE). The sample contained 213 residues which is 100% of the natural sequence. Out of 213 residues 206 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):
This entry contains 1 unique UniProt protein: