2foq

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|PDB= 2foq |SIZE=350|CAPTION= <scene name='initialview01'>2foq</scene>, resolution 1.25&Aring;
|PDB= 2foq |SIZE=350|CAPTION= <scene name='initialview01'>2foq</scene>, resolution 1.25&Aring;
|SITE=
|SITE=
-
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=B15:[2,2'-({4-[({2-[4-(AMINOSULFONYL)PHENYL]ETHYL}AMINO)CARBONYL]BENZYL}IMINO)DIACETATO(2-)-KAPPAO]COPPER'>B15</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=B15:[2,2&#39;-({4-[({2-[4-(AMINOSULFONYL)PHENYL]ETHYL}AMINO)CARBONYL]BENZYL}IMINO)DIACETATO(2-)-KAPPAO]COPPER'>B15</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</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= [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]
|GENE= CA2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
|GENE= CA2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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[[Category: zinc]]
[[Category: zinc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:55:01 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 15:06:44 2008''

Revision as of 13:06, 23 March 2008

Image:2foq.gif


PDB ID 2foq

Drag the structure with the mouse to rotate
, resolution 1.25Å
Ligands: , and
Gene: CA2 (Homo sapiens)
Activity: Carbonate dehydratase, with EC number 4.2.1.1
Coordinates: save as pdb, mmCIF, xml



Human Carbonic Anhydrase II complexed with two-prong inhibitors


Contents

Overview

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.

Disease

Known disease associated with this structure: Osteopetrosis, autosomal recessive 3, with renal tubular acidosis OMIM:[611492]

About this Structure

2FOQ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

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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