5d2b: Difference between revisions

Line 1:

~~'''Unreleased structure'''~~

~~The entry~~ 5d2b is ~~ON HOLD until Paper Publication~~

==Crystal structure of a mutated catalytic domain of Human MMP12 in complex with an hydroxamate analogue of RXP470==

~~Authors~~: ~~ROUANET~~-~~MEHOUAS~~, C., ~~DEVEL~~, L., ~~DIVE~~, V., ~~STURA~~, E.A.

== Structural highlights ==

<table><tr><td colspan='2'>[[5d2b]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D2B OCA]. For a guided tour on the structure components use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5D2B FirstGlance].

~~Description~~: ~~Crystal structure of~~ a ~~mutated catalytic domain of Human MMP12 in complex~~ with ~~an hydroxamate analogue of RXP470~~

</td></tr><tr id='ligand'><td class="sblockLbl">[[Ligand|Ligands:]]</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: ~~Unreleased Structures~~]]

<tr id='activity'><td class="sblockLbl">Activity:</td><td class="sblockDat">[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] </td></tr>

[[Category: ~~Dive~~, V]]

<tr id='resources'><td class="sblockLbl">Resources:</td><td class="sblockDat">[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5d2b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d2b OCA], [http://pdbe.org/5d2b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5d2b RCSB], [http://www.ebi.ac.uk/pdbsum/5d2b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5d2b ProSAT]</td></tr>

[[Category: ~~Devel~~, L]]

</table>

[[Category: ~~Rouanet~~-~~Mehouas~~, C]]

== Function ==

[[Category: ~~Stura~~, E.A]]

[[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: ROUANET-MEHOUAS, C]]

[[Category: STURA, E A]]

[[Category: Human]]

[[Category: Hydrolase]]

[[Category: Hydroxamate based inhibitor]]

[[Category: Macrophage]]

[[Category: Matrix metallo elastase]]

[[Category: Metzincin]]

[[Category: Mmp12]]

[[Category: Rxp470]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5d2b is ON HOLD  until Paper Publication
+==Crystal structure of a mutated catalytic domain of Human MMP12 in complex with an hydroxamate analogue of RXP470==
+<StructureSection load='5d2b' size='340' side='right' caption='[[5d2b]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
-Authors: ROUANET-MEHOUAS, C., DEVEL, L., DIVE, V., STURA, E.A.
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5d2b]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D2B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5D2B FirstGlance]. <br>
-Description: Crystal structure of a mutated catalytic domain of Human MMP12 in complex with an hydroxamate analogue of RXP470
+</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: Unreleased Structures]]
+<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>
-[[Category: Dive, V]]
+<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=5d2b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d2b OCA], [http://pdbe.org/5d2b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5d2b RCSB], [http://www.ebi.ac.uk/pdbsum/5d2b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5d2b ProSAT]</span></td></tr>
-[[Category: Devel, L]]
+</table>
-[[Category: Rouanet-Mehouas, C]]
+== Function ==
-[[Category: Stura, E.A]]
+[[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: ROUANET-MEHOUAS, C]]
+[[Category: STURA, E A]]
+[[Category: Human]]
+[[Category: Hydrolase]]
+[[Category: Hydroxamate based inhibitor]]
+[[Category: Macrophage]]
+[[Category: Matrix metallo elastase]]
+[[Category: Metzincin]]
+[[Category: Mmp12]]
+[[Category: Rxp470]]