1hld

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|PDB= 1hld |SIZE=350|CAPTION= <scene name='initialview01'>1hld</scene>, resolution 2.1&Aring;
|PDB= 1hld |SIZE=350|CAPTION= <scene name='initialview01'>1hld</scene>, resolution 2.1&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=PFB:2,3,4,5,6-PENTAFLUOROBENZYL+ALCOHOL'>PFB</scene> and <scene name='pdbligand=BRB:PARA-BROMOBENZYL ALCOHOL'>BRB</scene>
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|LIGAND= <scene name='pdbligand=BRB:PARA-BROMOBENZYL+ALCOHOL'>BRB</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=PFB:2,3,4,5,6-PENTAFLUOROBENZYL+ALCOHOL'>PFB</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Alcohol_dehydrogenase Alcohol dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.1 1.1.1.1]
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Alcohol_dehydrogenase Alcohol dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.1 1.1.1.1] </span>
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hld FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hld OCA], [http://www.ebi.ac.uk/pdbsum/1hld PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hld RCSB]</span>
}}
}}
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[[Category: Plapp, B V.]]
[[Category: Plapp, B V.]]
[[Category: Ramaswamy, S.]]
[[Category: Ramaswamy, S.]]
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[[Category: BRB]]
 
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[[Category: NAD]]
 
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[[Category: PFB]]
 
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[[Category: ZN]]
 
[[Category: oxidoreductase(ch-oh(d)-nad(a))]]
[[Category: oxidoreductase(ch-oh(d)-nad(a))]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:38:36 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:07:14 2008''

Revision as of 18:07, 30 March 2008


PDB ID 1hld

Drag the structure with the mouse to rotate
, resolution 2.1Å
Ligands: , , ,
Activity: Alcohol dehydrogenase, with EC number 1.1.1.1
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



STRUCTURES OF HORSE LIVER ALCOHOL DEHYDROGENASE COMPLEXED WITH NAD+ AND SUBSTITUTED BENZYL ALCOHOLS


Overview

Structures of the enzyme complexed with NAD+ and 2,3,4,5,6-pentafluorobenzyl alcohol were determined by X-ray crystallography at a resolution of 2.1 A and to a refinement R value of 18.3% for a monoclinic (P2(1)) form and to 2.4 A and an R value of 18.9% for a triclinic crystal form. The pentafluorobenzyl alcohol does not react, due to electron withdrawal by the fluorine atoms. A structure with NAD+ and p-bromobenzyl alcohol in the monoclinic form was also determined at 2.5 A and an R value of 16.7%. The conformations of the subunits in the monoclinic and triclinic crystal forms are very similar. The dimer is the asymmetric unit, and a rigid body rotation closes the cleft between the coenzyme and catalytic domains upon complex formation. In the monoclinic form, this conformational change is described by a rotation of 9 degrees in one subunit and 10 degrees in the other. The pentafluoro- and p-bromobenzyl alcohols bind in overlapping positions. The hydroxyl group of each alcohol is ligated to the catalytic zinc and participates in an extensive hydrogen-bonded network that includes the imidazole group of His-51, which can act as a base and shuttle a proton to solvent. The hydroxymethyl carbon of the pentafluorobenzyl alcohol is 3.4 A from C4 of the nicotinamide ring, and the pro-R hydrogen is in a good position for direct transfer to C4. The p-bromobenzyl alcohol may react after small rotations around single bonds of the alcohol. These structures should approximate the active Michaelis-Menten complexes.

About this Structure

1HLD is a Single protein structure of sequence from Equus caballus. Full crystallographic information is available from OCA.

Reference

Structures of horse liver alcohol dehydrogenase complexed with NAD+ and substituted benzyl alcohols., Ramaswamy S, Eklund H, Plapp BV, Biochemistry. 1994 May 3;33(17):5230-7. PMID:8172897

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