Your browser does not support inline frames or is currently configured not to display inline frames. Content can be viewed at actual source page: inc/head.html
PDBsum entry 1qlh
Go to PDB code:
Oxidoreductase
PDB id
1qlh
Loading ...
Contents
Protein chain
374 a.a.
*
Ligands
NAD
Metals
_ZN
×2
Waters
×88
*
Residue conservation analysis
PDB id:
1qlh
Links
PDBe
RCSB
MMDB
JenaLib
Proteopedia
CATH
SCOP
PDBSWS
PDBePISA
CSA
PROCOGNATE
ProSAT
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
Headers
References
Protein chain
?
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
'); } }