1CPO
CHLOROPEROXIDASE
Summary for 1CPO
| Entry DOI | 10.2210/pdb1cpo/pdb |
| Descriptor | CHLOROPEROXIDASE, alpha-D-mannopyranose-(1-3)-alpha-D-xylopyranose-(1-6)-[alpha-D-xylopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (10 entities in total) |
| Functional Keywords | hydrogen-peroxide oxidoreductase, heme peroxidase, haloperoxidase, oxidoreductase |
| Biological source | Leptoxyphium fumago |
| Total number of polymer chains | 1 |
| Total formula weight | 37160.64 |
| Authors | Sundaramoorthy, M.,Poulos, T.L. (deposition date: 1996-02-10, release date: 1997-02-12, Last modification date: 2024-10-09) |
| Primary citation | Sundaramoorthy, M.,Terner, J.,Poulos, T.L. The crystal structure of chloroperoxidase: a heme peroxidase--cytochrome P450 functional hybrid. Structure, 3:1367-1377, 1995 Cited by PubMed Abstract: Chloroperoxidase (CPO) is a versatile heme-containing enzyme that exhibits peroxidase, catalase and cytochrome P450-like activities in addition to catalyzing halogenation reactions. The structure determination of CPO was undertaken to help elucidate those structural features that enable the enzyme to exhibit these multiple activities. PubMed: 8747463DOI: 10.1016/S0969-2126(01)00274-X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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