2CAB

STRUCTURE, REFINEMENT AND FUNCTION OF CARBONIC ANHYDRASE ISOZYMES. REFINEMENT OF HUMAN CARBONIC ANHYDRASE I

Replaces:  1CAB

Summary for 2CAB

• Entry DOI: 10.2210/pdb2cab/pdb
• Descriptor: CARBONIC ANHYDRASE FORM B, ZINC ION (2 entities in total)
• Functional Keywords: hydro-lyase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: P00915
• Total number of polymer chains: 1
• Total formula weight: 28854.42

Authors

Kannan, K.K.,Ramanadham, M.,Jones, T.A. (deposition date: 1983-10-05, release date: 1984-02-02, Last modification date: 2024-02-14)

Primary citation

Kannan, K.K.,Ramanadham, M.,Jones, T.A.
Structure, refinement, and function of carbonic anhydrase isozymes: refinement of human carbonic anhydrase I
Ann.N.Y.Acad.Sci., 429:49-60, 1984

PubMed Abstract: The structure of human erythrocyte carbonic anhydrase I has been refined to a final R value of 19% to 2-A resolution by a combination of least squares refinement and model fitting in a three-dimensional graphics display. About 300 solvent atoms have been located bound to the protein molecule. An interesting hydrogen bond network involving Zn2+, the liganded solvent, side chain groups of Thr-199, Glu-106, Thr-7, and His-64 through two solvent molecules have been found that may be important for the catalytic mechanism of the carbonic anhydrase.

PubMed: 6430186

Experimental method

X-RAY DIFFRACTION (2 Å)