2foy: Difference between revisions
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|PDB= 2foy |SIZE=350|CAPTION= <scene name='initialview01'>2foy</scene>, resolution 1.55Å | |PDB= 2foy |SIZE=350|CAPTION= <scene name='initialview01'>2foy</scene>, resolution 1.55Å | ||
|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= <scene name='pdbligand=B30:{2,2'-[(2-{[4-(AMINOSULFONYL)BENZOYL]AMINO}ETHYL)IMINO]DIACETATO(2-)-KAPPAO}COPPER'>B30</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Carbonate_dehydratase Carbonate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.1 4.2.1.1] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Carbonate_dehydratase Carbonate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.1 4.2.1.1] </span> | ||
|GENE= CA1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= CA1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1hcb|1HCB]], [[2fov|2FOV]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2foy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2foy OCA], [http://www.ebi.ac.uk/pdbsum/2foy PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2foy RCSB]</span> | |||
}} | }} | ||
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[[Category: Roy, B.]] | [[Category: Roy, B.]] | ||
[[Category: Srivastava, D K.]] | [[Category: Srivastava, D K.]] | ||
[[Category: copper]] | [[Category: copper]] | ||
[[Category: inhibitor]] | [[Category: inhibitor]] | ||
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[[Category: zinc]] | [[Category: zinc]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:05:51 2008'' |
Revision as of 03:05, 31 March 2008
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, resolution 1.55Å | |||||||
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Ligands: | , | ||||||
Gene: | CA1 (Homo sapiens) | ||||||
Activity: | Carbonate dehydratase, with EC number 4.2.1.1 | ||||||
Related: | 1HCB, 2FOV
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Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Human Carbonic Anhydrase I complexed with a two-prong inhibitor
OverviewOverview
The atomic-resolution crystal structures of human carbonic anhydrases I and II complexed with "two-prong" inhibitors are reported. Each inhibitor contains a benzenesulfonamide prong and a cupric iminodiacetate (IDA-Cu(2+)) prong separated by linkers of different lengths and compositions. The ionized NH(-) group of each benzenesulfonamide coordinates to the active site Zn(2+) ion; the IDA-Cu(2+) prong of the tightest-binding inhibitor, BR30, binds to H64 of CAII and H200 of CAI. This work provides the first evidence verifying the structural basis of nanomolar affinity measured for two-prong inhibitors targeting the carbonic anhydrases.
About this StructureAbout this Structure
2FOY is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Ultrahigh resolution crystal structures of human carbonic anhydrases I and II complexed with "two-prong" inhibitors reveal the molecular basis of high affinity., Jude KM, Banerjee AL, Haldar MK, Manokaran S, Roy B, Mallik S, Srivastava DK, Christianson DW, J Am Chem Soc. 2006 Mar 8;128(9):3011-8. PMID:16506782
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