Summary for 1CYO
| Entry DOI | 10.2210/pdb1cyo/pdb |
| Descriptor | CYTOCHROME B5, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total) |
| Functional Keywords | electron transport |
| Biological source | Bos taurus (cattle) |
| Cellular location | Endoplasmic reticulum membrane; Single-pass membrane protein; Cytoplasmic side: P00171 |
| Total number of polymer chains | 1 |
| Total formula weight | 11268.21 |
| Authors | Durley, R.C.E.,Mathews, F.S. (deposition date: 1994-08-03, release date: 1994-11-30, Last modification date: 2024-02-07) |
| Primary citation | Durley, R.C.,Mathews, F.S. Refinement and structural analysis of bovine cytochrome b5 at 1.5 A resolution. Acta Crystallogr.,Sect.D, 52:65-76, 1996 Cited by PubMed Abstract: The structure of bovine liver cytochrome b(5), a soluble 93-residue proteolytic fragment of a 16 kDa membrane-bound hemoprotein, initially solved at 2.0 A resolution, has been refined at 1.5 A using data collected on a diffractometer. Refinement to 2.0 A resolution used the Hendrickson-Konnert procedure PROLSQ and was then extended to 1.5 A resolution using the program PROFFT. Only residues 3-87 could be identified in the model and these residues together with 93 water molecules gave an agreement factor of R = 0.161 for data in the resolution range 1.5-5 A. The structure was finally refined using the program X-PLOR, which enabled alternate conformers to be modelled for several surface side chains. Residues 1 and 2 at the amino terminus of the protein and residue 88 near the carboxyl terminus could be identified from these electron-density maps. However the remaining disordered carboxy-terminal residues could not successfully be included in the model. A total of 117 solvent molecules were included in the final refinement to give R = 0.164 for the data between 1.5 and 10 A. PubMed: 15299727DOI: 10.1107/S0907444995007827 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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