1au8: Difference between revisions

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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0H8:N-(3-CARBOXYPROPANOYL)-L-VALYL-N-[(1R)-5-AMINO-1-PHOSPHONOPENTYL]-L-PROLINAMIDE'>0H8</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0H8:N-(3-CARBOXYPROPANOYL)-L-VALYL-N-[(1R)-5-AMINO-1-PHOSPHONOPENTYL]-L-PROLINAMIDE'>0H8</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cathepsin_G Cathepsin G], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.20 3.4.21.20] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cathepsin_G Cathepsin G], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.20 3.4.21.20] </span></td></tr>
<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=1au8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1au8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1au8 RCSB], [http://www.ebi.ac.uk/pdbsum/1au8 PDBsum]</span></td></tr>
<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=1au8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1au8 OCA], [http://pdbe.org/1au8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1au8 RCSB], [http://www.ebi.ac.uk/pdbsum/1au8 PDBsum]</span></td></tr>
</table>
</table>
== Function ==
== Function ==

Revision as of 04:46, 11 September 2015

HUMAN CATHEPSIN GHUMAN CATHEPSIN G

Structural highlights

1au8 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Activity:Cathepsin G, with EC number 3.4.21.20
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[CATG_HUMAN] Serine protease with trypsin- and chymotrypsin-like specificity. Cleaves complement C3. Has antibacterial activity against the Gram-negative bacterium P.aeruginosa, antibacterial activity is inhibited by LPS from P.aeruginosa, Z-Gly-Leu-Phe-CH2Cl and phenylmethylsulfonyl fluoride.[1] [2] [3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Avril LE, Di Martino-Ferrer M, Pignede G, Seman M, Gauthier F. Identification of the U-937 membrane-associated proteinase interacting with the V3 loop of HIV-1 gp120 as cathepsin G. FEBS Lett. 1994 May 23;345(1):81-6. PMID:8194606
  2. ↑ Maison CM, Villiers CL, Colomb MG. Proteolysis of C3 on U937 cell plasma membranes. Purification of cathepsin G. J Immunol. 1991 Aug 1;147(3):921-6. PMID:1861080
  3. ↑ Wasiluk KR, Skubitz KM, Gray BH. Comparison of granule proteins from human polymorphonuclear leukocytes which are bactericidal toward Pseudomonas aeruginosa. Infect Immun. 1991 Nov;59(11):4193-200. PMID:1937776

1au8, resolution 1.90Å

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