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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
A0005737cellular_componentcytoplasm
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
A1990362molecular_functionbutanol dehydrogenase (NAD+) activity
B0004022molecular_functionalcohol dehydrogenase (NAD+) activity
B0005737cellular_componentcytoplasm
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
B1990362molecular_functionbutanol dehydrogenase (NAD+) activity
C0004022molecular_functionalcohol dehydrogenase (NAD+) activity
C0005737cellular_componentcytoplasm
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
C1990362molecular_functionbutanol dehydrogenase (NAD+) activity
D0004022molecular_functionalcohol dehydrogenase (NAD+) activity
D0005737cellular_componentcytoplasm
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
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: BINDING => ECO:0000269|PubMed:32596590, ECO:0007744|PDB:4Z6K
ChainResidueDetails
ACYS38
BHIS61
BGLU62
BCYS92
BCYS95
BCYS98
BCYS106
BCYS148
CCYS38
CHIS61
CGLU62
AHIS61
CCYS92
CCYS95
CCYS98
CCYS106
CCYS148
DCYS38
DHIS61
DGLU62
DCYS92
DCYS95
AGLU62
DCYS98
DCYS106
DCYS148
ACYS92
ACYS95
ACYS98
ACYS106
ACYS148
BCYS38

219140

PDB entries from 2024-05-01

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