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Summary Structural Experimental Function Sequence Neighbor Download Link


<Asymmetric unit>
= <Biological unit>

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PDB ID3efi  sequence information (FASTA format)   
DescriptorCarbonic anhydrase 2 (E.C.4.2.1.1)
TitleCarbonic anhydrase activators: Kinetic and X-ray crystallographic study for the interaction of d- and l-tryptophan with the mammalian isoforms I-XIV
Functional Keywordscarbonic anhydrase, activators, crystal structure, aminoacids, OXO-ACID, Acetylation, Cytoplasm, Disease mutation, Lyase, Metal-binding, Polymorphism, Zinc
LYASE
Biological source [UNP - P00918] Homo sapiens (Human)
Cellular location [UNP - P00918] Cytoplasm
Organ source [UNP - P00918] Ovary
Total number of polymer chains1
Total molecular weight29880.6 (the details in Structural Details Page)
AuthorsTemperini, C. , Innocenti, A. , Scozzafava, A. , Supuran, C.T. (deposition date : 2008-09-09, release date : 2008-09-30)
Primary citationTemperini, C. , Innocenti, A. , Scozzafava, A. , Supuran, C.T.
Carbonic anhydrase activators: kinetic and X-ray crystallographic study for the interaction of D- and L-tryptophan with the mammalian isoforms I-XIV
Bioorg.Med.Chem., 16:8373 - 8378, 2008.(PubMed : 18774300)  (DOI: 10.1016/j.bmc.2008.08.043)
Experimental methodX-RAY DIFFRACTION ( 1.75[Å] )
Other Database Information
Yorodumi , CATH , CE , FSSP , SCOP , VAST , UniProt ( P00918 ) , eF-site , KEGG ( EC 4.2.1.1 ) , PISA