4FWY
F33Y CuB myoglobin (F33Y L29H F43H sperm whale myoglobin) with copper bound
Summary for 4FWY
Entry DOI | 10.2210/pdb4fwy/pdb |
Related | 4FWX 4FWZ |
Descriptor | Myoglobin, PROTOPORPHYRIN IX CONTAINING FE, COPPER (II) ION, ... (4 entities in total) |
Functional Keywords | globin, oxidase, transport protein |
Biological source | Physeter catodon (Sperm whale) |
Total number of polymer chains | 1 |
Total formula weight | 18201.13 |
Authors | Gao, Y.-G.,Robinson, H.,Petrik, I.D.,Miner, K.D.,Lu, Y. (deposition date: 2012-07-02, release date: 2012-07-18, Last modification date: 2023-09-13) |
Primary citation | Miner, K.D.,Mukherjee, A.,Gao, Y.G.,Null, E.L.,Petrik, I.D.,Zhao, X.,Yeung, N.,Robinson, H.,Lu, Y. A Designed Functional Metalloenzyme that Reduces O(2) to H(2) O with Over One Thousand Turnovers. Angew.Chem.Int.Ed.Engl., 51:5589-5592, 2012 Cited by PubMed Abstract: [Image: see text] Rational design of functional enzymes with high turnovers is a significant challenge, especially those with complex active site and difficult reactions, such as in respiratory oxidases. Introducing 2 His and 1 Tyr into myoglobin resulted in designed enzymes that reduce O to HO with > 1000 turnovers and minimal release of reactive oxygen species. This also showed that presence and positioning of Tyr, not Cu, are critical for activity. PubMed: 22539151DOI: 10.1002/anie.201201981 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
Download full validation report
