1gve
From Proteopedia
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|PDB= 1gve |SIZE=350|CAPTION= <scene name='initialview01'>1gve</scene>, resolution 1.38Å | |PDB= 1gve |SIZE=350|CAPTION= <scene name='initialview01'>1gve</scene>, resolution 1.38Å | ||
|SITE= <scene name='pdbsite=AC1:Cit+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Cit+Binding+Site+For+Chain+A'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gve FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gve OCA], [http://www.ebi.ac.uk/pdbsum/1gve PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gve RCSB]</span> | ||
}} | }} | ||
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[[Category: Kozma, E.]] | [[Category: Kozma, E.]] | ||
[[Category: Lapthorn, A J.]] | [[Category: Lapthorn, A J.]] | ||
| - | [[Category: CIT]] | ||
| - | [[Category: GOL]] | ||
| - | [[Category: NAP]] | ||
[[Category: aflatoxin b1]] | [[Category: aflatoxin b1]] | ||
[[Category: akr7 family]] | [[Category: akr7 family]] | ||
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[[Category: succinic semialdehyde oxidoreductase]] | [[Category: succinic semialdehyde oxidoreductase]] | ||
| - | ''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 20:52:08 2008'' |
Revision as of 17:52, 30 March 2008
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| , resolution 1.38Å | |||||||
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| Sites: | |||||||
| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
AFLATOXIN ALDEHYDE REDUCTASE (AKR7A1) FROM RAT LIVER
Overview
The structure of the rat liver aflatoxin dialdehyde reductase (AKR7A1) has been solved to 1.38-A resolution. Although it shares a similar alpha/beta-barrel structure with other members of the aldo-keto reductase superfamily, AKR7A1 is the first dimeric member to be crystallized. The crystal structure also reveals details of the ternary complex as one subunit of the dimer contains NADP(+) and the inhibitor citrate. Although the underlying catalytic mechanism appears similar to other aldo-keto reductases, the substrate-binding pocket contains several charged amino acids (Arg-231 and Arg-327) that distinguish it from previously characterized aldo-keto reductases with respect to size and charge. These differences account for the substrate specificity for 4-carbon acid-aldehydes such as succinic semialdehyde and 2-carboxybenzaldehyde as well as for the idiosyncratic substrate aflatoxin B(1) dialdehyde of this subfamily of enzymes. Structural differences between the AKR7A1 ternary complex and apoenzyme reveal a significant hinged movement of the enzyme involving not only the loops of the structure but also parts of the alpha/beta-barrel most intimately involved in cofactor binding.
About this Structure
1GVE is a Protein complex structure of sequences from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
The crystal structure of rat liver AKR7A1. A dimeric member of the aldo-keto reductase superfamily., Kozma E, Brown E, Ellis EM, Lapthorn AJ, J Biol Chem. 2002 May 3;277(18):16285-93. Epub 2002 Feb 11. PMID:11839745
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