1UGE
HUMAN CARBONIC ANHYDRASE II [HCAII] (E.C.4.2.1.1) MUTANT WITH ALA 65 REPLACED BY LEU (A65L)
Summary for 1UGE
| Entry DOI | 10.2210/pdb1uge/pdb |
| Descriptor | CARBONIC ANHYDRASE II, MERCURY (II) ION, ZINC ION, ... (4 entities in total) |
| Functional Keywords | lyase, acetylation, zinc, polymorphism, disease mutation |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm: P00918 |
| Total number of polymer chains | 1 |
| Total formula weight | 29378.87 |
| Authors | Scolnick, L.R.,Christianson, D.W. (deposition date: 1996-07-24, release date: 1997-04-01, Last modification date: 2024-04-03) |
| Primary citation | Scolnick, L.R.,Christianson, D.W. X-ray crystallographic studies of alanine-65 variants of carbonic anhydrase II reveal the structural basis of compromised proton transfer in catalysis. Biochemistry, 35:16429-16434, 1996 Cited by PubMed: 8987974DOI: 10.1021/bi9617872 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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