5d3c: Difference between revisions
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==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: 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 03:00, 10 September 2016
Crystal structure of a double mutant catalytic domain of Human MMP12 in complex with an hydroxamate analogue of RXP470Crystal structure of a double mutant catalytic domain of Human MMP12 in complex with an hydroxamate analogue of RXP470
Structural highlights
Function[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. |
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