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6TQM

Escherichia coli AdhE structure in its compact conformation

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004022molecular_functionalcohol dehydrogenase (NAD+) activity
A0005515molecular_functionprotein binding
A0005829cellular_componentcytosol
A0006066biological_processalcohol metabolic process
A0006115biological_processethanol biosynthetic process
A0006979biological_processresponse to oxidative stress
A0008198molecular_functionferrous iron binding
A0008774molecular_functionacetaldehyde dehydrogenase (acetylating) activity
A0015976biological_processcarbon utilization
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
A0019664biological_processmixed acid fermentation
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A0051260biological_processprotein homooligomerization
A0120542molecular_functionethanol dehydrogenase (NAD+) activity
B0003824molecular_functioncatalytic activity
B0004022molecular_functionalcohol dehydrogenase (NAD+) activity
B0005515molecular_functionprotein binding
B0005829cellular_componentcytosol
B0006066biological_processalcohol metabolic process
B0006115biological_processethanol biosynthetic process
B0006979biological_processresponse to oxidative stress
B0008198molecular_functionferrous iron binding
B0008774molecular_functionacetaldehyde dehydrogenase (acetylating) activity
B0015976biological_processcarbon utilization
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
B0019664biological_processmixed acid fermentation
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
B0051260biological_processprotein homooligomerization
B0120542molecular_functionethanol dehydrogenase (NAD+) activity
C0003824molecular_functioncatalytic activity
C0004022molecular_functionalcohol dehydrogenase (NAD+) activity
C0005515molecular_functionprotein binding
C0005829cellular_componentcytosol
C0006066biological_processalcohol metabolic process
C0006115biological_processethanol biosynthetic process
C0006979biological_processresponse to oxidative stress
C0008198molecular_functionferrous iron binding
C0008774molecular_functionacetaldehyde dehydrogenase (acetylating) activity
C0015976biological_processcarbon utilization
C0016020cellular_componentmembrane
C0016491molecular_functionoxidoreductase activity
C0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
C0019664biological_processmixed acid fermentation
C0042802molecular_functionidentical protein binding
C0046872molecular_functionmetal ion binding
C0051260biological_processprotein homooligomerization
C0120542molecular_functionethanol dehydrogenase (NAD+) activity
F0003824molecular_functioncatalytic activity
F0004022molecular_functionalcohol dehydrogenase (NAD+) activity
F0005515molecular_functionprotein binding
F0005829cellular_componentcytosol
F0006066biological_processalcohol metabolic process
F0006115biological_processethanol biosynthetic process
F0006979biological_processresponse to oxidative stress
F0008198molecular_functionferrous iron binding
F0008774molecular_functionacetaldehyde dehydrogenase (acetylating) activity
F0015976biological_processcarbon utilization
F0016020cellular_componentmembrane
F0016491molecular_functionoxidoreductase activity
F0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
F0019664biological_processmixed acid fermentation
F0042802molecular_functionidentical protein binding
F0046872molecular_functionmetal ion binding
F0051260biological_processprotein homooligomerization
F0120542molecular_functionethanol dehydrogenase (NAD+) activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue FE B 901
ChainResidue
BASP653
BHIS657
BHIS723
BHIS737

site_idAC2
Number of Residues13
Detailsbinding site for residue NAI B 902
ChainResidue
BASP550
BTHR597
BSER603
BPHE608
BALA609
BLEU646
BHIS727
BHIS737
BASP487
BLEU490
BGLY545
BGLY546
BSER547

site_idAC3
Number of Residues4
Detailsbinding site for residue FE A 901
ChainResidue
AASP653
AHIS657
AHIS723
AHIS737

site_idAC4
Number of Residues13
Detailsbinding site for residue NAI A 902
ChainResidue
AASP487
ALEU490
AGLY545
AGLY546
ASER547
AASP550
ATHR597
ASER603
APHE608
AALA609
ALEU646
AHIS727
AHIS737

Functional Information from PROSITE/UniProt
site_idPS00060
Number of Residues21
DetailsADH_IRON_2 Iron-containing alcohol dehydrogenases signature 2. GvCHsmAHkLGSqfhIpHGlA
ChainResidueDetails
FGLY720-ALA740

site_idPS00913
Number of Residues29
DetailsADH_IRON_1 Iron-containing alcohol dehydrogenases signature 1. AIvDanlvmdmPkslcAfGglDAVthamE
ChainResidueDetails
FALA632-GLU660

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues50
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"32523125","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7BVP","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"32188856","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32523125","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"6TQH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6TQM","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues876
DetailsRegion: {"description":"Aldehyde dehydrogenase","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues14
DetailsRegion: {"description":"Linker","evidences":[{"source":"PubMed","id":"31586059","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"UniProtKB","id":"Q9HTJ1","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

248335

PDB entries from 2026-01-28

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