1bvd: Difference between revisions

Revision as of 19:46, 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:1bvd.png

Template:STRUCTURE 1bvd

STRUCTURE OF A BILIVERDIN APOMYOGLOBIN COMPLEX (FORM B) AT 98 KSTRUCTURE OF A BILIVERDIN APOMYOGLOBIN COMPLEX (FORM B) AT 98 K

Template:ABSTRACT PUBMED 7707378

About this StructureAbout this Structure

1BVD is a Single protein structure of sequence from Physeter catodon. Full crystallographic information is available from OCA.

ReferenceReference

Structure determination of the biliverdin apomyoglobin complex: crystal structure analysis of two crystal forms at 1.4 and 1.5 A resolution., Wagner UG, Muller N, Schmitzberger W, Falk H, Kratky C, J Mol Biol. 1995 Mar 24;247(2):326-37. PMID:7707378

Page seeded by OCA on Mon Jun 30 19:46:32 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1bvd.gif|left|200px]]
+{{Seed}}
+[[Image:1bvd.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1bvd|  PDB=1bvd  |  SCENE=  }}
-'''STRUCTURE OF A BILIVERDIN APOMYOGLOBIN COMPLEX (FORM B) AT 98 K'''
+===STRUCTURE OF A BILIVERDIN APOMYOGLOBIN COMPLEX (FORM B) AT 98 K===
-==Overview==
+<!--
-Crystal structure determinations of two orthorhombic (P2(1)2(1)2(1)) crystal modifications of the biliverdin apomyoglobin complex are described. The two structures were determined by X-ray diffraction at 100 K to a resolution of 1.5 A and 1.4 A. Both crystal forms were grown by hanging-drop techniques, using phosphate as precipitant. The structures were solved by molecular replacement and refined to final R-values of 19.4% and 21.2%. Both structures are very similar with respect to the binding site and the conformation of the biliverdin chromophore, which occurs in a (P) helical conformation. It is located within the heme pocket, very close in position and orientation to the heme binding site in myoglobin. Two water molecules not present in the crystal structure of myoglobin are sequestered within the heme pocket in the biliverdin-apomyoglobin complex, and they are engaged in hydrogen bonding to the biliverdin and to the protein. Comparison with structural results from an earlier NMR study of the same complex shows good agreement.
+The line below this paragraph, {{ABSTRACT_PUBMED_7707378}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 7707378 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_7707378}}
 ==About this Structure==
@@ Line 28: / Line 32: @@
 [[Category: Wagner, U G.]]
 [[Category: Oxygen storage]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 11:59:50 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:46:32 2008''