1YMC
THREE-DIMENSIONAL STRUCTURE OF CYANOMET-SULFMYOGLOBIN C
Summary for 1YMC
| Entry DOI | 10.2210/pdb1ymc/pdb |
| Descriptor | CYANOMET-SULFMYOGLOBIN, SULFATE ION, CYANIDE ION, ... (5 entities in total) |
| Functional Keywords | oxygen transport |
| Biological source | Equus caballus (horse) |
| Total number of polymer chains | 1 |
| Total formula weight | 17754.15 |
| Authors | Evans, S.V.,Brayer, G.D. (deposition date: 1993-09-27, release date: 1994-01-31, Last modification date: 2024-02-14) |
| Primary citation | Evans, S.V.,Sishta, B.P.,Mauk, A.G.,Brayer, G.D. Three-dimensional structure of cyanomet-sulfmyoglobin C. Proc.Natl.Acad.Sci.USA, 91:4723-4726, 1994 Cited by PubMed Abstract: The atomic structure of horse heart cyanomet-sulfmyoglobin C has been established by x-ray crystallographic techniques to a resolution of 2.0 A with an R value of 0.129. The protoheme IX prosthetic group of this thermodynamically stable sulfmyoglobin derivative has been converted to a chlorin in which the pyrrole ring bearing the 4-vinyl group is saturated and possesses an exocyclic thiolene ring. This study provides the three-dimensional structure of a protein with an iron-chlorin prosthetic group. The overall conformation of the surrounding polypeptide chain of the modified protein is very similar to that of the native protein. However, the addition of the sulfur atom has caused a distortion of the prosthetic group from that in the native protein to result in the repositioning of the side chains of some residues in the heme pocket. PubMed: 8197124DOI: 10.1073/pnas.91.11.4723 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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