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1lbu
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1lbu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_albus Streptomyces albus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LBU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LBU FirstGlance]. <br> | <table><tr><td colspan='2'>[[1lbu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_albus Streptomyces albus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LBU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LBU FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Muramoylpentapeptide_carboxypeptidase Muramoylpentapeptide carboxypeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.17.8 3.4.17.8] </span></td></tr> | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Muramoylpentapeptide_carboxypeptidase Muramoylpentapeptide carboxypeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.17.8 3.4.17.8] </span></td></tr> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lbu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lbu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1lbu RCSB], [http://www.ebi.ac.uk/pdbsum/1lbu 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=1lbu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lbu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1lbu RCSB], [http://www.ebi.ac.uk/pdbsum/1lbu PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/CBPM_STRAL CBPM_STRAL]] This enzyme catalyzes carboxypeptidation and transpeptidation reactions involved in bacterial cell wall metabolism. It effectively catalyzes the transfer of the N-alpha, N-epsilon-diacetyl-L-lysyl-D-alanyl electrophilic group of the standard tripeptide substrate N-alpha,N-epsilon-diacetyl-L-lysyl-D-alanyl-D-alanine to water. It also performs a weak beta-lactamase activity, hydrolyzing penicillin into penicilloate at a very low rate. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Muramoylpentapeptide carboxypeptidase]] | [[Category: Muramoylpentapeptide carboxypeptidase]] | ||
[[Category: Streptomyces albus]] | [[Category: Streptomyces albus]] | ||
| - | [[Category: Charlier, P | + | [[Category: Charlier, P]] |
| - | [[Category: Dideberg, O | + | [[Category: Dideberg, O]] |
| - | [[Category: Frere, J M | + | [[Category: Frere, J M]] |
| - | [[Category: Wery, J P | + | [[Category: Wery, J P]] |
[[Category: Carboxypeptidase]] | [[Category: Carboxypeptidase]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Nuclear receptor]] | [[Category: Nuclear receptor]] | ||
Revision as of 05:13, 25 December 2014
HYDROLASE METALLO (ZN) DD-PEPTIDASE
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