Bifunctional coenzyme A synthase (CoA synthase) Structure Main: Difference between revisions
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=='''Binding Sites and types for AcetylCoenzymeA ligand to CoenzymeA:'''== | =='''Binding Sites and types for AcetylCoenzymeA ligand to CoenzymeA:'''== | ||
'''Hydrophilic binding sites''' | '''Hydrophilic binding sites'''<BR> | ||
[[Image:COASYAcohydrophilicres.JPG]] | [[Image:COASYAcohydrophilicres.JPG]] | ||
[[Image:COASYAcohydrophilic.JPG]] | [[Image:COASYAcohydrophilic.JPG]] | ||
'''Hydrophobic binding sites''' | '''Hydrophobic binding sites'''<BR> | ||
[[Image:COASYAcohydrophobicres.JPG]] | [[Image:COASYAcohydrophobicres.JPG]] | ||
[[Image:COASYAcohydrophobic.JPG]] | [[Image:COASYAcohydrophobic.JPG]] | ||
'''Bridged H bond binding sites''' | '''Bridged H bond binding sites'''<BR> | ||
[[Image:COASYAcobridgedhbond.JPG]] | [[Image:COASYAcobridgedhbond.JPG]] | ||
'''Other binding sites''' | '''Other binding sites'''<BR> | ||
[[Image:COASYAcootherres.JPG]] | [[Image:COASYAcootherres.JPG]] | ||
[[Image:COASYAcoother.JPG]] | [[Image:COASYAcoother.JPG]] |
Revision as of 06:36, 15 May 2007
Coenzyme A Atomic structures:
Coenzyme A atomic structure by bfactor (flexibility as denoted by crystalography; red is more flexible, blue is more structurally stable)
Coenzyme A Ribbon structures:
Coenzyme A ribbon structure with water molecules
Coenzyme A ribbon structure by hydrophobicity
Coenzyme A ribbon structure by compound type
Coenzyme A ribbon structure by conformation/structural type
Binding Sites and types for AcetylCoenzymeA ligand to CoenzymeA:
Binding Sites and types for unknown ligand UNL to CoenzymeA:
Highly Structurally Related Proteins:
Thymidylate Kinase: Nucleoside monophosphate kinase. Catalyses reversible phosphorylation transfer between ATP & TMP > ADP & TDP. Activates Anti HIV prodrugs.
Shikimate Kinase: Target for nontoxic antimicrobial agents, herbicides and parasite drugs. Absent in mammals. Catalyses reaction of phosphoryltransfer from ATP to shikimic acid.
Adenylate Kinase: Nucleoside monophosphate kinase. Essential for bacterial survival. AMP(bd) domain close to core of structure. Low catalytic activity compared to eukaryotic kinases (10 fold slower).
Dephospho-COA Kinase: Uses ATP as phosphate donor in phosphorylation of 3-hydroxy group of ribose (final stages of biosynthesis). ATP binds in p-loop (as it does in other kinases). COA binding site located at join of all 3 domains.
UMP/CMP kinase: Supplies precursors for nucleic acid synthesis. Catalyses UMP,CMP & dCMP into diphosphate form. Component of nucleoside analog prodrugs (AraC, gemcitabine & ddC).
Uridine-Cystidine Kinase: Catalyses phosphorylation of uridine & cystidine. Upon cystidine binding UCK becomes strictly specific to pyramidine ribnucleotides.