2fw4: Difference between revisions
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|PDB= 2fw4 |SIZE=350|CAPTION= <scene name='initialview01'>2fw4</scene>, resolution 2.00Å | |PDB= 2fw4 |SIZE=350|CAPTION= <scene name='initialview01'>2fw4</scene>, resolution 2.00Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=HIS:HISTIDINE'>HIS</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= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fw4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fw4 OCA], [http://www.ebi.ac.uk/pdbsum/2fw4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2fw4 RCSB]</span> | |||
}} | }} | ||
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[[Category: Supuran, C T.]] | [[Category: Supuran, C T.]] | ||
[[Category: Temperini, C.]] | [[Category: Temperini, C.]] | ||
[[Category: activator]] | [[Category: activator]] | ||
[[Category: carbonic anhydrase i]] | [[Category: carbonic anhydrase i]] | ||
[[Category: crystal structure]] | [[Category: crystal structure]] | ||
''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 03:08:33 2008'' | ||
Revision as of 00:08, 31 March 2008
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| 2fw4, resolution 2.00Å | |||||||||||||
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| Ligands: | HIS, ZN | ||||||||||||
| Activity: | Carbonate dehydratase, with EC number 4.2.1.1 | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Carbonic anhydrase activators. The first X-ray crystallographic study of an activator of isoform I, structure with L-histidine.
Overview
The X-ray crystallographic structure for the adduct of an activator with human carbonic anhydrase isozyme I (hCA I) is reported. L-Histidine binds deep within the enzyme active site, participating in a network of hydrogen bonds involving its carboxylate moiety and the zinc-bound water molecule, as well as the imidazole of His200, being in van der Waals contacts with Thr199, His200, His64, and His67. This binding is very different from that to the other major cytosolic isozyme hCA II.
About this Structure
2FW4 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Carbonic anhydrase activators: the first X-ray crystallographic study of an adduct of isoform I., Temperini C, Scozzafava A, Supuran CT, Bioorg Med Chem Lett. 2006 Oct 1;16(19):5152-6. Epub 2006 Jul 25. PMID:16870440
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