1au8: Difference between revisions

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<StructureSection load='1au8' size='340' side='right'caption='[[1au8]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='1au8' size='340' side='right'caption='[[1au8]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1au8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AU8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AU8 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1au8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AU8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AU8 FirstGlance]. <br>
</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" id="ligandDat"><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'>[https://en.wikipedia.org/wiki/Cathepsin_G Cathepsin G], with EC number [https://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://pdbe.org/1au8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1au8 RCSB], [http://www.ebi.ac.uk/pdbsum/1au8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1au8 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1au8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1au8 OCA], [https://pdbe.org/1au8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1au8 RCSB], [https://www.ebi.ac.uk/pdbsum/1au8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1au8 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/CATG_HUMAN 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.<ref>PMID:8194606</ref> <ref>PMID:1861080</ref> <ref>PMID:1937776</ref>   
[[https://www.uniprot.org/uniprot/CATG_HUMAN 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.<ref>PMID:8194606</ref> <ref>PMID:1861080</ref> <ref>PMID:1937776</ref>   
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]

Revision as of 18:01, 2 June 2021

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, ProSAT

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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