1hld: Difference between revisions
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[[Image:1hld.jpg|left|200px]] | [[Image:1hld.jpg|left|200px]] | ||
'''STRUCTURES OF HORSE LIVER ALCOHOL DEHYDROGENASE COMPLEXED WITH NAD+ AND SUBSTITUTED BENZYL ALCOHOLS''' | {{Structure | ||
|PDB= 1hld |SIZE=350|CAPTION= <scene name='initialview01'>1hld</scene>, resolution 2.1Å | |||
|SITE= | |||
|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> | |||
|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] | |||
|GENE= | |||
}} | |||
'''STRUCTURES OF HORSE LIVER ALCOHOL DEHYDROGENASE COMPLEXED WITH NAD+ AND SUBSTITUTED BENZYL ALCOHOLS''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1HLD is a [ | 1HLD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HLD OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8172897 8172897] | ||
[[Category: Alcohol dehydrogenase]] | [[Category: Alcohol dehydrogenase]] | ||
[[Category: Equus caballus]] | [[Category: Equus caballus]] | ||
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[[Category: oxidoreductase(ch-oh(d)-nad(a))]] | [[Category: oxidoreductase(ch-oh(d)-nad(a))]] | ||
''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 11:38:36 2008'' | ||
Revision as of 09:38, 20 March 2008
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| 1hld, resolution 2.1Å | |||||||||||||
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| Ligands: | ZN, NAD, PFB and BRB | ||||||||||||
| Activity: | Alcohol dehydrogenase, with EC number 1.1.1.1 | ||||||||||||
| 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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