1ymc
From Proteopedia
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THREE-DIMENSIONAL STRUCTURE OF CYANOMET-SULFMYOGLOBIN C
Overview
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.
About this Structure
1YMC is a Single protein structure of sequence from Equus caballus with SO4, CYN and CLN as ligands. Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of cyanomet-sulfmyoglobin C., Evans SV, Sishta BP, Mauk AG, Brayer GD, Proc Natl Acad Sci U S A. 1994 May 24;91(11):4723-6. PMID:8197124
Page seeded by OCA on Wed Nov 21 06:54:31 2007
Categories: Equus caballus | Single protein | Brayer, G.D. | Evans, S.V. | CLN | CYN | SO4 | Oxygen transport
