1ZSA
CARBONIC ANHYDRASE II MUTANT E117Q, APO FORM
Summary for 1ZSA
Entry DOI | 10.2210/pdb1zsa/pdb |
Descriptor | CARBONIC ANHYDRASE II (2 entities in total) |
Functional Keywords | lyase, oxo-acid, acetylation, zinc, polymorphism, lyase (oxo-acid) |
Biological source | Homo sapiens (human) |
Cellular location | Cytoplasm: P00918 |
Total number of polymer chains | 1 |
Total formula weight | 29156.88 |
Authors | Lesburg, C.A.,Christianson, D.W. (deposition date: 1996-01-09, release date: 1996-07-11, Last modification date: 2024-02-14) |
Primary citation | Huang, C.C.,Lesburg, C.A.,Kiefer, L.L.,Fierke, C.A.,Christianson, D.W. Reversal of the hydrogen bond to zinc ligand histidine-119 dramatically diminishes catalysis and enhances metal equilibration kinetics in carbonic anhydrase II. Biochemistry, 35:3439-3446, 1996 Cited by PubMed: 8639494DOI: 10.1021/bi9526692 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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