5d2b

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (11:24, 10 January 2024) (edit) (undo)
 
(2 intermediate revisions not shown.)
Line 1: Line 1:
==Crystal structure of a mutated catalytic domain of Human MMP12 in complex with an hydroxamate analogue of RXP470==
==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=''>
+
<StructureSection load='5d2b' size='340' side='right'caption='[[5d2b]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
== Structural highlights ==
== 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>
+
<table><tr><td colspan='2'>[[5d2b]] 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=5D2B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5D2B 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>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.2&#8491;</td></tr>
-
<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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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>
-
<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>
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5d2b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d2b OCA], [https://pdbe.org/5d2b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5d2b RCSB], [https://www.ebi.ac.uk/pdbsum/5d2b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5d2b ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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.
+
[https://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.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Line 19: Line 19:
</div>
</div>
<div class="pdbe-citations 5d2b" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 5d2b" style="background-color:#fffaf0;"></div>
 +
 +
==See Also==
 +
*[[Matrix metalloproteinase 3D structures|Matrix metalloproteinase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Macrophage elastase]]
+
[[Category: Homo sapiens]]
-
[[Category: DEVEL, L]]
+
[[Category: Large Structures]]
-
[[Category: DIVE, V]]
+
[[Category: Devel L]]
-
[[Category: ROUANET-MEHOUAS, C]]
+
[[Category: Dive V]]
-
[[Category: STURA, E A]]
+
[[Category: Rouanet-Mehouas C]]
-
[[Category: Human]]
+
[[Category: Stura EA]]
-
[[Category: Hydrolase]]
+
-
[[Category: Hydroxamate based inhibitor]]
+
-
[[Category: Macrophage]]
+
-
[[Category: Matrix metallo elastase]]
+
-
[[Category: Metzincin]]
+
-
[[Category: Mmp12]]
+
-
[[Category: Rxp470]]
+

Current revision

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

PDB ID 5d2b

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5d2b"
Personal tools