1gz6
From Proteopedia
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|PDB= 1gz6 |SIZE=350|CAPTION= <scene name='initialview01'>1gz6</scene>, resolution 2.38Å | |PDB= 1gz6 |SIZE=350|CAPTION= <scene name='initialview01'>1gz6</scene>, resolution 2.38Å | ||
|SITE= <scene name='pdbsite=AC1:Nai+Binding+Site+For+Chain+C'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Nai+Binding+Site+For+Chain+C'>AC1</scene> | ||
- | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
- | |ACTIVITY= [http://en.wikipedia.org/wiki/Estradiol_17-beta-dehydrogenase Estradiol 17-beta-dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.62 1.1.1.62] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Estradiol_17-beta-dehydrogenase Estradiol 17-beta-dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.62 1.1.1.62] </span> |
|GENE= | |GENE= | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY= | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gz6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gz6 OCA], [http://www.ebi.ac.uk/pdbsum/1gz6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gz6 RCSB]</span> | ||
}} | }} | ||
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[[Category: Haapalainen, A M.]] | [[Category: Haapalainen, A M.]] | ||
[[Category: Hiltunen, J K.]] | [[Category: Hiltunen, J K.]] | ||
- | [[Category: NAI]] | ||
- | [[Category: SO4]] | ||
[[Category: 17beta-hsd4]] | [[Category: 17beta-hsd4]] | ||
[[Category: beta-oxidation]] | [[Category: beta-oxidation]] | ||
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[[Category: steroid biosynthesis]] | [[Category: steroid biosynthesis]] | ||
- | ''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 20:54:24 2008'' |
Revision as of 17:54, 30 March 2008
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, resolution 2.38Å | |||||||
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Sites: | |||||||
Ligands: | , , | ||||||
Activity: | Estradiol 17-beta-dehydrogenase, with EC number 1.1.1.62 | ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
(3R)-HYDROXYACYL-COA DEHYDROGENASE FRAGMENT OF RAT PEROXISOMAL MULTIFUNCTIONAL ENZYME TYPE 2
Overview
The crystal structure of (3R)-hydroxyacyl-CoA dehydrogenase of rat peroxisomal multifunctional enzyme type 2 (MFE-2) was solved at 2.38 A resolution. The catalytic entity reveals an alpha/beta short chain alcohol dehydrogenase/reductase (SDR) fold and the conformation of the bound nicotinamide adenine dinucleotide (NAD(+)) found in other SDR enzymes. Of great interest is the separate COOH-terminal domain, which is not seen in other SDR structures. This domain completes the active site cavity of the neighboring monomer and extends dimeric interactions. Peroxisomal diseases that arise because of point mutations in the dehydrogenase-coding region of the MFE-2 gene can be mapped to changes in amino acids involved in NAD(+) binding and protein dimerization.
About this Structure
1GZ6 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Binary structure of the two-domain (3R)-hydroxyacyl-CoA dehydrogenase from rat peroxisomal multifunctional enzyme type 2 at 2.38 A resolution., Haapalainen AM, Koski MK, Qin YM, Hiltunen JK, Glumoff T, Structure. 2003 Jan;11(1):87-97. PMID:12517343
Page seeded by OCA on Sun Mar 30 20:54:24 2008