1p0c
From Proteopedia
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|PDB= 1p0c |SIZE=350|CAPTION= <scene name='initialview01'>1p0c</scene>, resolution 2.2Å | |PDB= 1p0c |SIZE=350|CAPTION= <scene name='initialview01'>1p0c</scene>, resolution 2.2Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Alcohol_dehydrogenase_(NADP(+)) Alcohol dehydrogenase (NADP(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.2 1.1.1.2] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Alcohol_dehydrogenase_(NADP(+)) Alcohol dehydrogenase (NADP(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.2 1.1.1.2] </span> |
| - | |GENE= ADH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id= | + | |GENE= ADH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8403 Rana perezi]) |
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1p0f|1P0F]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1p0c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p0c OCA], [http://www.ebi.ac.uk/pdbsum/1p0c PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1p0c RCSB]</span> | ||
}} | }} | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1P0C is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ | + | 1P0C is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rana_perezi Rana perezi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P0C OCA]. |
==Reference== | ==Reference== | ||
Crystal structure of the vertebrate NADP(H)-dependent alcohol dehydrogenase (ADH8)., Rosell A, Valencia E, Pares X, Fita I, Farres J, Ochoa WF, J Mol Biol. 2003 Jun 27;330(1):75-85. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12818203 12818203] | Crystal structure of the vertebrate NADP(H)-dependent alcohol dehydrogenase (ADH8)., Rosell A, Valencia E, Pares X, Fita I, Farres J, Ochoa WF, J Mol Biol. 2003 Jun 27;330(1):75-85. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12818203 12818203] | ||
[[Category: Alcohol dehydrogenase (NADP(+))]] | [[Category: Alcohol dehydrogenase (NADP(+))]] | ||
| - | [[Category: Rana | + | [[Category: Rana perezi]] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Farres, J.]] | [[Category: Farres, J.]] | ||
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[[Category: Rosell, A.]] | [[Category: Rosell, A.]] | ||
[[Category: Valencia, E.]] | [[Category: Valencia, E.]] | ||
| - | [[Category: GOL]] | ||
| - | [[Category: PO4]] | ||
| - | [[Category: ZN]] | ||
[[Category: adh topology]] | [[Category: adh topology]] | ||
[[Category: nadp(h)-dependent]] | [[Category: nadp(h)-dependent]] | ||
| - | ''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 22:52:55 2008'' |
Revision as of 19:52, 30 March 2008
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| , resolution 2.2Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Gene: | ADH (Rana perezi) | ||||||
| Activity: | Alcohol dehydrogenase (NADP(+)), with EC number 1.1.1.2 | ||||||
| Related: | 1P0F
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of the NADP(H)-Dependent Vertebrate Alcohol Dehydrogenase (ADH8)
Overview
The amphibian enzyme ADH8, previously named class IV-like, is the only known vertebrate alcohol dehydrogenase (ADH) with specificity towards NADP(H). The three-dimensional structures of ADH8 and of the binary complex ADH8-NADP(+) have been now determined and refined to resolutions of 2.2A and 1.8A, respectively. The coenzyme and substrate specificity of ADH8, that has 50-65% sequence identity with vertebrate NAD(H)-dependent ADHs, suggest a role in aldehyde reduction probably as a retinal reductase. The large volume of the substrate-binding pocket can explain both the high catalytic efficiency of ADH8 with retinoids and the high K(m) value for ethanol. Preference of NADP(H) appears to be achieved by the presence in ADH8 of the triad Gly223-Thr224-His225 and the recruitment of conserved Lys228, which define a binding pocket for the terminal phosphate group of the cofactor. NADP(H) binds to ADH8 in an extended conformation that superimposes well with the NAD(H) molecules found in NAD(H)-dependent ADH complexes. No additional reshaping of the dinucleotide-binding site is observed which explains why NAD(H) can also be used as a cofactor by ADH8. The structural features support the classification of ADH8 as an independent ADH class.
About this Structure
1P0C is a Single protein structure of sequence from Rana perezi. Full crystallographic information is available from OCA.
Reference
Crystal structure of the vertebrate NADP(H)-dependent alcohol dehydrogenase (ADH8)., Rosell A, Valencia E, Pares X, Fita I, Farres J, Ochoa WF, J Mol Biol. 2003 Jun 27;330(1):75-85. PMID:12818203
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