1dvg
From Proteopedia
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|PDB= 1dvg |SIZE=350|CAPTION= <scene name='initialview01'>1dvg</scene>, resolution 2.20Å | |PDB= 1dvg |SIZE=350|CAPTION= <scene name='initialview01'>1dvg</scene>, resolution 2.20Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN IX CONTAINING FE'>HEM</scene> | + | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Heme_oxygenase Heme oxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.99.3 1.14.99.3] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Heme_oxygenase Heme oxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.99.3 1.14.99.3] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1qq8|1QQ8]], [[1dve|1DVE]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dvg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dvg OCA], [http://www.ebi.ac.uk/pdbsum/1dvg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dvg RCSB]</span> | ||
}} | }} | ||
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[[Category: Sakamoto, H.]] | [[Category: Sakamoto, H.]] | ||
[[Category: Sugishima, M.]] | [[Category: Sugishima, M.]] | ||
| - | [[Category: HEM]] | ||
[[Category: all alpha]] | [[Category: all alpha]] | ||
[[Category: protein-substrate complex]] | [[Category: protein-substrate complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:49:30 2008'' |
Revision as of 16:49, 30 March 2008
| |||||||
| , resolution 2.20Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Heme oxygenase, with EC number 1.14.99.3 | ||||||
| Related: | 1QQ8, 1DVE
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF RAT HEME OXYGENASE-1 IN COMPLEX WITH HEME; SELELENO-METHIONINE DERIVATIVE, MUTATED AT M51T,M93L,M155L,M191L.
Overview
Heme oxygenase catalyzes the oxidative cleavage of protoheme to biliverdin, the first step of heme metabolism utilizing O(2) and NADPH. We determined the crystal structures of rat heme oxygenase-1 (HO-1)-heme and selenomethionyl HO-1-heme complexes. Heme is sandwiched between two helices with the delta-meso edge of the heme being exposed to the surface. Gly143N forms a hydrogen bond to the distal ligand of heme, OH(-). The distance between Gly143N and the ligand is shorter than that in the human HO-1-heme complex. This difference may be related to a pH-dependent change of the distal ligand of heme. Flexibility of the distal helix may control the stability of the coordination of the distal ligand to heme iron. The possible role of Gly143 in the heme oxygenase reaction is discussed.
About this Structure
1DVG is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Crystal structure of rat heme oxygenase-1 in complex with heme., Sugishima M, Omata Y, Kakuta Y, Sakamoto H, Noguchi M, Fukuyama K, FEBS Lett. 2000 Apr 7;471(1):61-6. PMID:10760513
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