6f02: Difference between revisions
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==Crystal structure of human glycosylated kallistatin at 3.0 Angstrom resolution== | |||
<StructureSection load='6f02' size='340' side='right' caption='[[6f02]], [[Resolution|resolution]] 3.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6f02]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6F02 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6F02 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=FUL:BETA-L-FUCOSE'>FUL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |||
[[Category: | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6f02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f02 OCA], [http://pdbe.org/6f02 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6f02 RCSB], [http://www.ebi.ac.uk/pdbsum/6f02 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6f02 ProSAT]</span></td></tr> | ||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/KAIN_HUMAN KAIN_HUMAN]] Inhibits human amidolytic and kininogenase activities of tissue kallikrein. Inhibition is achieved by formation of an equimolar, heat- and SDS-stable complex between the inhibitor and the enzyme, and generation of a small C-terminal fragment of the inhibitor due to cleavage at the reactive site by tissue kallikrein.<ref>PMID:8227002</ref> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Ma, L]] | |||
[[Category: Zhou, A]] | [[Category: Zhou, A]] | ||
[[Category: | [[Category: Heparin]] | ||
[[Category: Hydrolase]] | |||
[[Category: Inhibitor]] | |||
[[Category: Kallilrein]] | |||
[[Category: Protease]] | |||
[[Category: Serine protease inhibitor]] |
Revision as of 09:47, 12 December 2018
Crystal structure of human glycosylated kallistatin at 3.0 Angstrom resolutionCrystal structure of human glycosylated kallistatin at 3.0 Angstrom resolution
Structural highlights
Function[KAIN_HUMAN] Inhibits human amidolytic and kininogenase activities of tissue kallikrein. Inhibition is achieved by formation of an equimolar, heat- and SDS-stable complex between the inhibitor and the enzyme, and generation of a small C-terminal fragment of the inhibitor due to cleavage at the reactive site by tissue kallikrein.[1] References |
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