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==Crystal structure of MhuD R26S mutant with two hemes bound per active site== | |||
<StructureSection load='6ds7' size='340' side='right'caption='[[6ds7]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6ds7]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DS7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6DS7 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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/Heme_oxygenase_(biliverdin-producing) Heme oxygenase (biliverdin-producing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.14.18 1.14.14.18] </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=6ds7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ds7 OCA], [http://pdbe.org/6ds7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ds7 RCSB], [http://www.ebi.ac.uk/pdbsum/6ds7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ds7 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/MHUD_MYCTU MHUD_MYCTU]] Catalyzes the oxidative degradation of the heme macrocyclic porphyrin ring in the presence of a suitable electron donor such as ascorbate or NADPH--cytochrome P450 reductase, with subsequent release of free iron. | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Chao, A]] | |||
[[Category: Goulding, C W]] | |||
[[Category: Cell wall]] | |||
[[Category: Heme binding]] | |||
[[Category: Heme catabolic process]] | |||
[[Category: Metal ion binding]] | |||
[[Category: Monooxygenase activity]] | |||
[[Category: Oxidation reduction process]] | |||
[[Category: Oxidoreductase]] | |||
[[Category: Oxidoreductase activity]] | |||
[[Category: Plasma membrane]] |
Revision as of 08:50, 19 June 2019
Crystal structure of MhuD R26S mutant with two hemes bound per active siteCrystal structure of MhuD R26S mutant with two hemes bound per active site
Structural highlights
Function[MHUD_MYCTU] Catalyzes the oxidative degradation of the heme macrocyclic porphyrin ring in the presence of a suitable electron donor such as ascorbate or NADPH--cytochrome P450 reductase, with subsequent release of free iron. |
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