1cot: Difference between revisions

Revision as of 21:02, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1cot.png

Template:STRUCTURE 1cot

X-RAY STRUCTURE OF THE CYTOCHROME C2 ISOLATED FROM PARACOCCUS DENITRIFICANS REFINED TO 1.7 ANGSTROMS RESOLUTIONX-RAY STRUCTURE OF THE CYTOCHROME C2 ISOLATED FROM PARACOCCUS DENITRIFICANS REFINED TO 1.7 ANGSTROMS RESOLUTION

Template:ABSTRACT PUBMED 8179333

About this StructureAbout this Structure

1COT is a Single protein structure of sequence from Paracoccus denitrificans. Full crystallographic information is available from OCA.

ReferenceReference

X-Ray structure of the cytochrome c2 isolated from Paracoccus denitrificans refined to 1.7-A resolution., Benning MM, Meyer TE, Holden HM, Arch Biochem Biophys. 1994 May 1;310(2):460-6. PMID:8179333

Page seeded by OCA on Mon Jun 30 21:02:10 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1cot.jpg|left|200px]]
+{{Seed}}
+[[Image:1cot.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1cot|  PDB=1cot  |  SCENE=  }}
-'''X-RAY STRUCTURE OF THE CYTOCHROME C2 ISOLATED FROM PARACOCCUS DENITRIFICANS REFINED TO 1.7 ANGSTROMS RESOLUTION'''
+===X-RAY STRUCTURE OF THE CYTOCHROME C2 ISOLATED FROM PARACOCCUS DENITRIFICANS REFINED TO 1.7 ANGSTROMS RESOLUTION===
-==Overview==
+<!--
-The cytochrome c2 (formerly c550) isolated from Paracoccus denitrificans is one of the larger bacterial c-type proteins examined thus far. The molecular structure of this cytochrome has been redetermined and refined to 1.7-A resolution with a crystallographic R-factor of 17.5% for all measured X-ray data. Like other, smaller c-type cytochromes, the molecule consists of five alpha-helices that wrap around the heme group. In addition, this bacterial cytochrome contains two strands of anti-parallel beta-sheet, five Type I turns, and three Type II turns. The present model differs from the originally determined structure in several regions including the N-terminus, the loop delineated by Asp 25 to Lys 31, the region defined by Trp 86 to Val 88, and the C-terminus. A total of 103 water molecules has been positioned into the electron density map. Six of these waters are directly involved in heme binding.
+The line below this paragraph, {{ABSTRACT_PUBMED_8179333}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 8179333 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_8179333}}
 ==About this Structure==
@@ Line 26: / Line 30: @@
 [[Category: Meyer, T E.]]
 [[Category: Electron transport]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 12:57:29 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 21:02:10 2008''