1xww
From Proteopedia
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|PDB= 1xww |SIZE=350|CAPTION= <scene name='initialview01'>1xww</scene>, resolution 1.63Å | |PDB= 1xww |SIZE=350|CAPTION= <scene name='initialview01'>1xww</scene>, resolution 1.63Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= ACP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= ACP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[5pnt|5PNT]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xww FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xww OCA], [http://www.ebi.ac.uk/pdbsum/1xww PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1xww RCSB]</span> | ||
}} | }} | ||
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[[Category: Stauffacher, C V.]] | [[Category: Stauffacher, C V.]] | ||
[[Category: Zabell, A P.R.]] | [[Category: Zabell, A P.R.]] | ||
| - | [[Category: GOL]] | ||
| - | [[Category: SO4]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''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 00:55:45 2008'' |
Revision as of 21:55, 30 March 2008
| |||||||
| , resolution 1.63Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | ACP1 (Homo sapiens) | ||||||
| Related: | 5PNT
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of Human B-form Low Molecular Weight Phosphotyrosyl Phosphatase at 1.6 Angstrom Resolution
Overview
The crystal structure of HPTP-B, a human isoenzyme of the low molecular weight phosphotyrosyl phosphatase (LMW PTPase) is reported here at a resolution of 1.6 A. This high resolution structure of the second human LMW PTPase isoenzyme provides the opportunity to examine the structural basis of different substrate and inhibitor/activator responses. The crystal packing of HPTP-B positions a normally surface-exposed arginine in a position equivalent to the tyrosyl substrate. A comparison of all deposited crystallographic coordinates of these PTPases reveals three atomic positions within the active site cavity occupied by hydrogen bond donor or acceptor atoms on bound molecules, suggesting useful design elements for synthetic inhibitors. A selection of inhibitor and activator molecules as well as small molecule and peptide substrates were tested against each human isoenzyme. These results along with the crystal packing seen in HPTP-B suggest relevant sequence elements in the currently unknown target sequence.
About this Structure
1XWW is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of the human B-form low molecular weight phosphotyrosyl phosphatase at 1.6-A resolution., Zabell AP, Schroff AD Jr, Bain BE, Van Etten RL, Wiest O, Stauffacher CV, J Biol Chem. 2006 Mar 10;281(10):6520-7. Epub 2005 Oct 27. PMID:16253994
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