Summary for 1CA2
| Entry DOI | 10.2210/pdb1ca2/pdb |
| Descriptor | CARBONIC ANHYDRASE II, ZINC ION (3 entities in total) |
| Functional Keywords | lyase(oxo-acid) |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm : P00918 |
| Total number of polymer chains | 1 |
| Total formula weight | 29223.27 |
| Authors | Eriksson, A.E.,Jones, T.A.,Liljas, A. (deposition date: 1989-02-06, release date: 1990-01-15, Last modification date: 2024-02-07) |
| Primary citation | Eriksson, A.E.,Jones, T.A.,Liljas, A. Refined structure of human carbonic anhydrase II at 2.0 A resolution. Proteins, 4:274-282, 1988 Cited by PubMed Abstract: The structure of human erythrocytic carbonic anhydrase II has been refined by constrained and restrained structure-factor least-squares refinement at 2.0 A resolution. The conventional crystallographic R value is 17.3%. Of 167 solvent molecules associated with the protein, four are buried and stabilize secondary structure elements. The zinc ion is ligated to three histidyl residues and one water molecule in a nearly tetrahedral geometry. In addition to the zinc-bound water, seven more water molecules are identified in the active site. Assuming that Glu-106 is deprotonated at pH 8.5, some of the hydrogen bond donor-acceptor relations in the active site can be assigned and are described here in detail. The O gamma 1 atom of Thr-199 donates its proton to the O epsilon 1 atom of Glu-106 and can function as a hydrogen bond acceptor only in additional hydrogen bonds. PubMed: 3151019DOI: 10.1002/prot.340040406 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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