256b

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Template:STRUCTURE 256b

Contents

IMPROVEMENT OF THE 2.5 ANGSTROMS RESOLUTION MODEL OF CYTOCHROME B562 BY REDETERMINING THE PRIMARY STRUCTURE AND USING MOLECULAR GRAPHICS

About this Structure

256b is a 2 chain structure of Cytochrome b5 with sequence from Escherichia coli. This structure supersedes the now removed PDB entry 156b. Full crystallographic information is available from OCA.

See Also

Reference

  • Lederer F, Glatigny A, Bethge PH, Bellamy HD, Matthew FS. Improvement of the 2.5 A resolution model of cytochrome b562 by redetermining the primary structure and using molecular graphics. J Mol Biol. 1981 Jun 5;148(4):427-48. PMID:7031264
  • . PMID:007723042
  • Chou KC. Does the folding type of a protein depend on its amino acid composition? FEBS Lett. 1995 Apr 17;363(1-2):127-31. PMID:7729532
  • Parker MH, Hefford MA. A consensus residue analysis of loop and helix-capping residues in four-alpha-helical-bundle proteins. Protein Eng. 1997 May;10(5):487-96. PMID:9215566
  • Greene LH, Higman VA. Uncovering network systems within protein structures. J Mol Biol. 2003 Dec 5;334(4):781-91. PMID:14636602

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