1bmf: Difference between revisions
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|PDB= 1bmf |SIZE=350|CAPTION= <scene name='initialview01'>1bmf</scene>, resolution 2.85Å | |PDB= 1bmf |SIZE=350|CAPTION= <scene name='initialview01'>1bmf</scene>, resolution 2.85Å | ||
|SITE= <scene name='pdbsite=CAT:The+Carboxylate+Group+Of+GLU+Residue+Is+Believed+To+Acti+...'>CAT</scene> and <scene name='pdbsite=PLP:LYS+Within+The+P-Loop+(Phosphate+Binding)+Motif,+Gxxxxgkt/S'>PLP</scene> | |SITE= <scene name='pdbsite=CAT:The+Carboxylate+Group+Of+GLU+Residue+Is+Believed+To+Acti+...'>CAT</scene> and <scene name='pdbsite=PLP:LYS+Within+The+P-Loop+(Phosphate+Binding)+Motif,+Gxxxxgkt/S'>PLP</scene> | ||
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene> and <scene name='pdbligand=ADP:ADENOSINE-5 | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene> and <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Transferred_entry:_3.6.3.14 Transferred entry: 3.6.3.14], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.34 3.6.1.34] | |ACTIVITY= [http://en.wikipedia.org/wiki/Transferred_entry:_3.6.3.14 Transferred entry: 3.6.3.14], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.34 3.6.1.34] | ||
|GENE= | |GENE= | ||
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[[Category: f1fo atp synthase]] | [[Category: f1fo atp synthase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 11:16:06 2008'' | ||
Revision as of 12:16, 23 March 2008
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| , resolution 2.85Å | |||||||
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| Sites: | and | ||||||
| Ligands: | , and | ||||||
| Activity: | Transferred entry: 3.6.3.14, with EC number 3.6.1.34 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
BOVINE MITOCHONDRIAL F1-ATPASE
OverviewOverview
In the crystal structure of bovine mitochondrial F1-ATPase determined at 2.8 A resolution, the three catalytic beta-subunits differ in conformation and in the bound nucleotide. The structure supports a catalytic mechanism in intact ATP synthase in which the three catalytic subunits are in different states of the catalytic cycle at any instant. Interconversion of the states may be achieved by rotation of the alpha 3 beta 3 subassembly relative to an alpha-helical domain of the gamma-subunit.
About this StructureAbout this Structure
1BMF is a Protein complex structure of sequences from Bos taurus. Full crystallographic information is available from OCA.
ReferenceReference
Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria., Abrahams JP, Leslie AG, Lutter R, Walker JE, Nature. 1994 Aug 25;370(6491):621-8. PMID:8065448
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