1n5d
From Proteopedia
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| - | [[Image:1n5d.gif|left|200px]] | + | [[Image:1n5d.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF PORCINE TESTICULAR CARBONYL REDUCTASE/ 20BETA-HYDROXYSTEROID DEHYDROGENASE''' | + | {{Structure |
| + | |PDB= 1n5d |SIZE=350|CAPTION= <scene name='initialview01'>1n5d</scene>, resolution 2.30Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=NDP:NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE'>NDP</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/3-alpha-(or_20-beta)-hydroxysteroid_dehydrogenase 3-alpha-(or 20-beta)-hydroxysteroid dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.53 1.1.1.53] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF PORCINE TESTICULAR CARBONYL REDUCTASE/ 20BETA-HYDROXYSTEROID DEHYDROGENASE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1N5D is a [ | + | 1N5D is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. This structure supersedes the now removed PDB entry 1HU4. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N5D OCA]. |
==Reference== | ==Reference== | ||
| - | Porcine carbonyl reductase. structural basis for a functional monomer in short chain dehydrogenases/reductases., Ghosh D, Sawicki M, Pletnev V, Erman M, Ohno S, Nakajin S, Duax WL, J Biol Chem. 2001 May 25;276(21):18457-63. Epub 2001 Mar 8. PMID:[http:// | + | Porcine carbonyl reductase. structural basis for a functional monomer in short chain dehydrogenases/reductases., Ghosh D, Sawicki M, Pletnev V, Erman M, Ohno S, Nakajin S, Duax WL, J Biol Chem. 2001 May 25;276(21):18457-63. Epub 2001 Mar 8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11279087 11279087] |
[[Category: 3-alpha-(or 20-beta)-hydroxysteroid dehydrogenase]] | [[Category: 3-alpha-(or 20-beta)-hydroxysteroid dehydrogenase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: shortchain dehydrogenase/reductase]] | [[Category: shortchain dehydrogenase/reductase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:52:21 2008'' |
Revision as of 10:52, 20 March 2008
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| , resolution 2.30Å | |||||||
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| Ligands: | and | ||||||
| Activity: | 3-alpha-(or 20-beta)-hydroxysteroid dehydrogenase, with EC number 1.1.1.53 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF PORCINE TESTICULAR CARBONYL REDUCTASE/ 20BETA-HYDROXYSTEROID DEHYDROGENASE
Overview
Porcine testicular carbonyl reductase (PTCR) belongs to the short chain dehydrogenases/reductases (SDR) superfamily and catalyzes the NADPH-dependent reduction of ketones on steroids and prostaglandins. The enzyme shares nearly 85% sequence identity with the NADPH-dependent human 15-hydroxyprostaglandin dehydrogenase/carbonyl reductase. The tertiary structure of the enzyme at 2.3 A reveals a fold characteristic of the SDR superfamily that uses a Tyr-Lys-Ser triad as catalytic residues, but exhibits neither the functional homotetramer nor the homodimer that distinguish all SDRs. It is the first known monomeric structure in the SDR superfamily. In PTCR, which is also active as a monomer, a 41-residue insertion immediately before the catalytic Tyr describes an all-helix subdomain that packs against interfacial helices, eliminating the four-helix bundle interface conserved in the superfamily. An additional anti-parallel strand in the PTCR structure also blocks the other strand-mediated interface. These novel structural features provide the basis for the scaffolding of one catalytic site within a single molecule of the enzyme.
About this Structure
1N5D is a Single protein structure of sequence from Sus scrofa. This structure supersedes the now removed PDB entry 1HU4. Full crystallographic information is available from OCA.
Reference
Porcine carbonyl reductase. structural basis for a functional monomer in short chain dehydrogenases/reductases., Ghosh D, Sawicki M, Pletnev V, Erman M, Ohno S, Nakajin S, Duax WL, J Biol Chem. 2001 May 25;276(21):18457-63. Epub 2001 Mar 8. PMID:11279087
Page seeded by OCA on Thu Mar 20 12:52:21 2008
