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4Z6K

Alcohol dehydrogenase from the antarctic psychrophile Moraxella sp. TAE 123

Functional Information from GO Data
ChainGOidnamespacecontents
A0004022molecular_functionalcohol dehydrogenase (NAD+) activity
A0008270molecular_functionzinc ion binding
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0046872molecular_functionmetal ion binding
A0120542molecular_functionethanol dehydrogenase (NAD+) activity
A1990362molecular_functionbutanol dehydrogenase (NAD+) activity
B0004022molecular_functionalcohol dehydrogenase (NAD+) activity
B0008270molecular_functionzinc ion binding
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0046872molecular_functionmetal ion binding
B0120542molecular_functionethanol dehydrogenase (NAD+) activity
B1990362molecular_functionbutanol dehydrogenase (NAD+) activity
C0004022molecular_functionalcohol dehydrogenase (NAD+) activity
C0008270molecular_functionzinc ion binding
C0016491molecular_functionoxidoreductase activity
C0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C0046872molecular_functionmetal ion binding
C0120542molecular_functionethanol dehydrogenase (NAD+) activity
C1990362molecular_functionbutanol dehydrogenase (NAD+) activity
D0004022molecular_functionalcohol dehydrogenase (NAD+) activity
D0008270molecular_functionzinc ion binding
D0016491molecular_functionoxidoreductase activity
D0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D0046872molecular_functionmetal ion binding
D0120542molecular_functionethanol dehydrogenase (NAD+) activity
D1990362molecular_functionbutanol dehydrogenase (NAD+) activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue ZN A 401
ChainResidue
ACYS38
AHIS61
AGLU62
ACYS148
AARG331

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN A 402
ChainResidue
ACYS92
ACYS95
ACYS98
ACYS106

site_idAC3
Number of Residues6
Detailsbinding site for residue ZN B 401
ChainResidue
BCYS38
BHIS61
BGLU62
BCYS148
BARG331
BHOH501

site_idAC4
Number of Residues4
Detailsbinding site for residue ZN B 402
ChainResidue
BCYS92
BCYS95
BCYS98
BCYS106

site_idAC5
Number of Residues4
Detailsbinding site for residue ZN B 403
ChainResidue
AHIS342
AHIS344
BHIS7
BGLU16

site_idAC6
Number of Residues5
Detailsbinding site for residue ZN C 401
ChainResidue
CCYS38
CHIS61
CGLU62
CCYS148
CARG331

site_idAC7
Number of Residues4
Detailsbinding site for residue ZN C 402
ChainResidue
CCYS92
CCYS95
CCYS98
CCYS106

site_idAC8
Number of Residues5
Detailsbinding site for residue ZN D 401
ChainResidue
DCYS38
DHIS61
DGLU62
DCYS148
DARG331

site_idAC9
Number of Residues4
Detailsbinding site for residue ZN D 402
ChainResidue
DCYS92
DCYS95
DCYS98
DCYS106

site_idAD1
Number of Residues4
Detailsbinding site for residue ZN D 403
ChainResidue
CHIS342
CHIS344
DHIS7
DGLU16

Functional Information from PROSITE/UniProt
site_idPS00059
Number of Residues15
DetailsADH_ZINC Zinc-containing alcohol dehydrogenases signature. GHEgVGLitavGegV
ChainResidueDetails
AGLY60-VAL74

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues32
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"32596590","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4Z6K","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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