5d3c
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of a double mutant catalytic domain of Human MMP12 in complex with an hydroxamate analogue of RXP470== | |
| - | + | <StructureSection load='5d3c' size='340' side='right' caption='[[5d3c]], [[Resolution|resolution]] 1.31Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5d3c]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D3C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5D3C FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=56O:N-[(2R)-2-{[3-(3-CHLOROBIPHENYL-4-YL)-1,2-OXAZOL-5-YL]METHYL}-4-(HYDROXYAMINO)-4-OXOBUTANOYL]-L-ALPHA-GLUTAMYL-L-ALPHA-GLUTAMINE'>56O</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |
| - | [[Category: | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Macrophage_elastase Macrophage elastase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.65 3.4.24.65] </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=5d3c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d3c OCA], [http://pdbe.org/5d3c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5d3c RCSB], [http://www.ebi.ac.uk/pdbsum/5d3c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5d3c ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/MMP12_HUMAN MMP12_HUMAN]] May be involved in tissue injury and remodeling. Has significant elastolytic activity. Can accept large and small amino acids at the P1' site, but has a preference for leucine. Aromatic or hydrophobic residues are preferred at the P1 site, with small hydrophobic residues (preferably alanine) occupying P3. | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Macrophage elastase]] | ||
| + | [[Category: Devel, L]] | ||
[[Category: Dive, V]] | [[Category: Dive, V]] | ||
| - | [[Category: Devel, L]] | ||
[[Category: Rouanet-Mehouas, C]] | [[Category: Rouanet-Mehouas, C]] | ||
| - | [[Category: Stura, E | + | [[Category: Stura, E A]] |
| + | [[Category: Human]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Hydroxamate]] | ||
| + | [[Category: Macrophage metalloelastase]] | ||
| + | [[Category: Mmp12]] | ||
| + | [[Category: Rxp470]] | ||
Revision as of 00:00, 10 September 2016
Crystal structure of a double mutant catalytic domain of Human MMP12 in complex with an hydroxamate analogue of RXP470
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