Summary for 3CYT
| Entry DOI | 10.2210/pdb3cyt/pdb |
| Descriptor | CYTOCHROME C, HEME C (3 entities in total) |
| Functional Keywords | electron transport (heme protein) |
| Biological source | Thunnus alalunga (albacore) |
| Cellular location | Mitochondrion intermembrane space: P81459 |
| Total number of polymer chains | 2 |
| Total formula weight | 24069.23 |
| Authors | Takano, T. (deposition date: 1980-07-01, release date: 1980-09-16, Last modification date: 2024-10-23) |
| Primary citation | Takano, T.,Dickerson, R.E. Redox conformation changes in refined tuna cytochrome c. Proc.Natl.Acad.Sci.USA, 77:6371-6375, 1980 Cited by PubMed Abstract: Tuna ferrocytochrome c and ferricytochrome c have been refined independently at high resolution (1.5 A and 1.8 A) to crystallographic residual errors of 17.3% and 20.8%, respectively. Small but significant conformational differences are seen surrounding a buried water molecule that is hydrogen bonded to Asn-52, Tyr-67, and Thr-78. In the oxidized state, this water molecule is 1.0 A closer to the heme and the heme has moved 0.15 A out of its heme crevice; both changes lead to a more polar microenvironment for the heme. Chemical modification studies, patterns of evolutionary conservatism, structural differences in bacterial cytochromes, and x-ray studies all agree that the "active site" for cytochrome c is bounded by lysines 8, 13,27, 72, 79, 86, and 87 (thus containing the evolutionary conservative 72-87 loop) and has the buried water molecule just below its surface and the opening of the heme crevice slightly to one side. PubMed: 6256733DOI: 10.1073/pnas.77.11.6371 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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