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PDBsum entry 1qlh

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protein ligands metals links
Oxidoreductase PDB id
1qlh

 

 

 

 

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Contents
Protein chain
374 a.a. *
Ligands
NAD
Metals
_ZN ×2
Waters ×88
* Residue conservation analysis
PDB id:
1qlh
Name: Oxidoreductase
Title: Horse liver alcohol dehydrogenase complexed to NAD double mutant of gly 293 ala and pro 295 thr
Structure: Alcohol dehydrogenase. Chain: a. Synonym: adh, alcohol dehydrogenase e chain. Engineered: yes. Mutation: yes
Source: Equus caballus. Horse. Organism_taxid: 9796. Organ: liver. Cellular_location: cytoplasm. Expressed in: escherichia coli. Expression_system_taxid: 562. Other_details: e.Coli expressed mutant protein
Biol. unit: Dimer (from PDB file)
Resolution:
2.07Å     R-factor:   0.209     R-free:   0.254
Authors: S.Ramaswamy,B.V.Plapp
Date:
31-Aug-99     Release date:   02-Jan-00    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P00327  (ADH1E_HORSE) -  Alcohol dehydrogenase E chain from Equus caballus
Seq:
Struc:
375 a.a.
374 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.1.1.1.1  - alcohol dehydrogenase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction:
1. a primary alcohol + NAD+ = an aldehyde + NADH + H+
2. a secondary alcohol + NAD+ = a ketone + NADH + H+
primary alcohol
+
NAD(+)
Bound ligand (Het Group name = NAD)
matches with 97.73% similarity
= aldehyde
+ NADH
+ H(+)
secondary alcohol
+
NAD(+)
Bound ligand (Het Group name = NAD)
matches with 97.73% similarity
= ketone
+ NADH
+ H(+)
      Cofactor: Zn(2+) or Fe cation
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

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