1bvd: Difference between revisions
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|PDB= 1bvd |SIZE=350|CAPTION= <scene name='initialview01'>1bvd</scene>, resolution 1.4Å | |PDB= 1bvd |SIZE=350|CAPTION= <scene name='initialview01'>1bvd</scene>, resolution 1.4Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=BLA:BILIVERDINE IX ALPHA'>BLA</scene> | |LIGAND= <scene name='pdbligand=BLA:BILIVERDINE+IX+ALPHA'>BLA</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bvd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bvd OCA], [http://www.ebi.ac.uk/pdbsum/1bvd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bvd RCSB]</span> | |||
}} | }} | ||
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[[Category: Schmitzberger, W.]] | [[Category: Schmitzberger, W.]] | ||
[[Category: Wagner, U G.]] | [[Category: Wagner, U G.]] | ||
[[Category: oxygen storage]] | [[Category: oxygen storage]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:09:01 2008'' | ||
Revision as of 19:09, 30 March 2008
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF A BILIVERDIN APOMYOGLOBIN COMPLEX (FORM B) AT 98 K
OverviewOverview
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.
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
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