1QAF
THE ACTIVE SITE BASE CONTROLS COFACTOR REACTIVITY IN ESCHERICHIA COLI AMINE OXIDASE : X-RAY CRYSTALLOGRAPHIC STUDIES WITH MUTATIONAL VARIANTS
Summary for 1QAF
Entry DOI | 10.2210/pdb1qaf/pdb |
Descriptor | PROTEIN (COPPER AMINE OXIDASE), COPPER (II) ION, CALCIUM ION, ... (5 entities in total) |
Functional Keywords | catalytic domain mainly anti-parallel beta sheet, three peripheral alpha-beta domains, oxidoreductase |
Biological source | Escherichia coli |
Cellular location | Periplasm: P46883 |
Total number of polymer chains | 2 |
Total formula weight | 161977.75 |
Authors | Murray, J.M.,Wilmot, C.M.,Saysell, C.G.,Jaeger, J.,Knowles, P.F.,Phillips, S.E.,McPherson, M.J. (deposition date: 1999-03-11, release date: 1999-08-23, Last modification date: 2023-08-16) |
Primary citation | Murray, J.M.,Saysell, C.G.,Wilmot, C.M.,Tambyrajah, W.S.,Jaeger, J.,Knowles, P.F.,Phillips, S.E.,McPherson, M.J. The active site base controls cofactor reactivity in Escherichia coli amine oxidase: x-ray crystallographic studies with mutational variants. Biochemistry, 38:8217-8227, 1999 Cited by PubMed: 10387067DOI: 10.1021/bi9900469 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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