Structure of PDB 1oj7 Chain C

Receptor sequence
>1oj7C (length=390) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
KAGLNNFNLHTPTRILFGKGAIAGLREQIPHDARVLITYGGGSVKKTGVL
DQVLDALKGMDVLEFGGIEPNPAYETLMNAVKLVREQKVTFLLAVGGGSV
LDGTKFIAAAANYPENIDPWHILQTGGKEIKSAIPMGCVLTLPATGSESN
AGAVISRKTTGDKQAFHSAHVQPVFAVLDPVYTYTLPPRQVANGVVDAFV
HTVEQYVTKPVDAKIHDRFAEGILLTLIEDGPKALKEPENYDVRANVMWA
ATQALNGLIGAGVPQDWATHMLGHELTAMHGLDHAQTLAIVLPALWNEKR
DTKRAKLLQYAERVWNITEGSDDERIDAAIAATRNFFEQLGVPTHLSDYG
LDGSSIPALLKKLEEHGMTQLGENHDITLDVSRRIYEAAR
3D structure
PDB1oj7 Crystal Structure of E.Coli Alcohol Dehydrogenase Yqhd: Evidence of a Covalently Modified Nadp Coenzyme
ChainC
Resolution2.0 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.1.1.2: alcohol dehydrogenase (NADP(+)).
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 ZN C D194 H198 H267 H281 D197 H201 H270 H284
Gene Ontology
Molecular Function
GO:0008106 alcohol dehydrogenase (NADP+) activity
GO:0008270 zinc ion binding
GO:0016491 oxidoreductase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0018455 alcohol dehydrogenase [NAD(P)+] activity
GO:0042802 identical protein binding
GO:0046872 metal ion binding
GO:1990002 methylglyoxal reductase (NADPH) (acetol producing) activity
GO:1990362 butanol dehydrogenase (NAD+) activity
Biological Process
GO:0000302 response to reactive oxygen species
Cellular Component
GO:0005829 cytosol

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:1oj7, PDBe:1oj7, PDBj:1oj7
PDBsum1oj7
PubMed15327949
UniProtQ46856|YQHD_ECOLI Alcohol dehydrogenase YqhD (Gene Name=yqhD)

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