1dws
From Proteopedia
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| - | [[Image:1dws.gif|left|200px]] | + | [[Image:1dws.gif|left|200px]] |
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| - | '''PHOTOLYZED CARBONMONOXY MYOGLOBIN (HORSE HEART)''' | + | {{Structure |
| + | |PDB= 1dws |SIZE=350|CAPTION= <scene name='initialview01'>1dws</scene>, resolution 1.45Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> and <scene name='pdbligand=CMO:CARBON MONOXIDE'>CMO</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''PHOTOLYZED CARBONMONOXY MYOGLOBIN (HORSE HEART)''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1DWS is a [ | + | 1DWS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DWS OCA]. |
==Reference== | ==Reference== | ||
| - | Structure of a ligand-binding intermediate in wild-type carbonmonoxy myoglobin., Chu K, Vojtchovsky J, McMahon BH, Sweet RM, Berendzen J, Schlichting I, Nature. 2000 Feb 24;403(6772):921-3. PMID:[http:// | + | Structure of a ligand-binding intermediate in wild-type carbonmonoxy myoglobin., Chu K, Vojtchovsky J, McMahon BH, Sweet RM, Berendzen J, Schlichting I, Nature. 2000 Feb 24;403(6772):921-3. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10706294 10706294] |
[[Category: Equus caballus]] | [[Category: Equus caballus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: respiratory protein]] | [[Category: respiratory protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:45:41 2008'' |
Revision as of 08:45, 20 March 2008
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| , resolution 1.45Å | |||||||
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| Ligands: | , and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
PHOTOLYZED CARBONMONOXY MYOGLOBIN (HORSE HEART)
Overview
Small molecules such as NO, O2, CO or H2 are important biological ligands that bind to metalloproteins to function crucially in processes such as signal transduction, respiration and catalysis. A key issue for understanding the regulation of reaction mechanisms in these systems is whether ligands gain access to the binding sites through specific channels and docking sites, or by random diffusion through the protein matrix. A model system for studying this issue is myoglobin, a simple haem protein. Myoglobin has been studied extensively by spectroscopy, crystallography, computation and theory. It serves as an aid to oxygen diffusion but also binds carbon monoxide, a byproduct of endogenous haem catabolism. Molecular dynamics simulations, random mutagenesis and flash photolysis studies indicate that ligand migration occurs through a limited number of pathways involving docking sites. Here we report the 1.4 A resolution crystal structure of a ligand-binding intermediate in carbonmonoxy myoglobin that may have far-reaching implications for understanding the dynamics of ligand binding and catalysis.
About this Structure
1DWS is a Single protein structure of sequence from Equus caballus. Full crystallographic information is available from OCA.
Reference
Structure of a ligand-binding intermediate in wild-type carbonmonoxy myoglobin., Chu K, Vojtchovsky J, McMahon BH, Sweet RM, Berendzen J, Schlichting I, Nature. 2000 Feb 24;403(6772):921-3. PMID:10706294
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