1yk4: Difference between revisions

Revision as of 10:59, 29 July 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:1yk4.png

Template:STRUCTURE 1yk4

Ultra-high resolution structure of Pyrococcus abyssi rubredoxin W4L/R5SUltra-high resolution structure of Pyrococcus abyssi rubredoxin W4L/R5S

Template:ABSTRACT PUBMED 15983423

About this StructureAbout this Structure

1YK4 is a Single protein structure of sequence from Pyrococcus abyssi. Full crystallographic information is available from OCA.

ReferenceReference

Ultrahigh-resolution study on Pyrococcus abyssi rubredoxin. I. 0.69 A X-ray structure of mutant W4L/R5S., Bonisch H, Schmidt CL, Bianco P, Ladenstein R, Acta Crystallogr D Biol Crystallogr. 2005 Jul;61(Pt 7):990-1004. Epub 2005, Jun 24. PMID:15983423

Page seeded by OCA on Tue Jul 29 10:59:31 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1yk4.gif|left|200px]]
+{{Seed}}
+[[Image:1yk4.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1yk4|  PDB=1yk4  |  SCENE=  }}
-'''Ultra-high resolution structure of Pyrococcus abyssi rubredoxin W4L/R5S'''
+===Ultra-high resolution structure of Pyrococcus abyssi rubredoxin W4L/R5S===
-==Overview==
+<!--
-The crystal structure of Pyrococcus abyssi rubredoxin mutant W4L/R5S was solved by direct methods. The model of the air-oxidized protein was refined by partially restrained full-matrix least-squares refinement against intensity data to 0.69 A resolution. This first ultrahigh-resolution structure of a rubredoxin provides very detailed and precise information about the Fe(SCys)(4) centre and its environment, the peptide-backbone stereochemistry, H atoms and hydrogen bonds, static and dynamic disorder, the solvent structure and the electron-density distribution. P. abyssi rubredoxin W4L/R5S is the first of a series of mutants studied by atomic and ultrahigh-resolution X-ray crystallography which are expected to contribute to the understanding of structure-function relationships in iron-sulfur proteins.
+The line below this paragraph, {{ABSTRACT_PUBMED_15983423}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15983423 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15983423}}
 ==About this Structure==
@@ Line 27: / Line 31: @@
 [[Category: Schmidt, C L.]]
 [[Category: Electron transport]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 16:25:19 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 10:59:31 2008''