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3PII

Crystal structure of Mutant of ht- Alcohol Dehydrogenase with substrate analogue butyramide

Functional Information from GO Data
ChainGOidnamespacecontents
A0004022molecular_functionalcohol dehydrogenase (NAD+) activity
A0005737cellular_componentcytoplasm
A0008270molecular_functionzinc ion binding
A0016491molecular_functionoxidoreductase activity
A0046872molecular_functionmetal ion binding
B0004022molecular_functionalcohol dehydrogenase (NAD+) activity
B0005737cellular_componentcytoplasm
B0008270molecular_functionzinc ion binding
B0016491molecular_functionoxidoreductase activity
B0046872molecular_functionmetal ion binding
C0004022molecular_functionalcohol dehydrogenase (NAD+) activity
C0005737cellular_componentcytoplasm
C0008270molecular_functionzinc ion binding
C0016491molecular_functionoxidoreductase activity
C0046872molecular_functionmetal ion binding
D0004022molecular_functionalcohol dehydrogenase (NAD+) activity
D0005737cellular_componentcytoplasm
D0008270molecular_functionzinc ion binding
D0016491molecular_functionoxidoreductase activity
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN D 340
ChainResidue
DCYS38
DHIS61
DGLU62
DCYS148
DBMD400

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 340
ChainResidue
BBMD500
BCYS38
BHIS61
BGLU62
BCYS148

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 340
ChainResidue
ACYS38
AHIS61
AGLU62
ACYS148
AARG331

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN C 340
ChainResidue
CCYS38
CHIS61
CGLU62
CCYS148
CARG331

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 341
ChainResidue
ACYS92
ACYS95
ACYS98
ACYS106

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 341
ChainResidue
CCYS92
CCYS95
CCYS98
CCYS106

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 341
ChainResidue
BCYS92
BGLY93
BCYS95
BCYS98
BCYS106

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN D 341
ChainResidue
DCYS92
DGLY93
DCYS95
DCYS98
DCYS106

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE BMD D 400
ChainResidue
DCYS38
DTHR40
DHIS61
DTRP87
DCYS148
DVAL286
DZN340

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE BMD B 500
ChainResidue
BTHR40
BHIS61
BTRP87
BCYS148
BVAL286
BZN340

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE BMD A 600
ChainResidue
ATHR40
AHIS61
ATRP87
ACYS148
AVAL286

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE BMD C 700
ChainResidue
CTHR40
CHIS61
CTRP87
CCYS148
CVAL286

site_idBC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 342
ChainResidue
AGLY175
APHE176
AHOH343

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 342
ChainResidue
BHIS39
BGLY174
BGLY175
BHOH343

site_idBC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 C 342
ChainResidue
CGLY174
CGLY175
CHOH343

site_idBC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 D 342
ChainResidue
DHIS39
DGLY174
DGLY175

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues48
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AASP195
ALYS200
AVAL260
AARG331
CCYS38
CHIS61
CCYS92
CCYS95
CCYS98
CCYS106
CCYS148
CGLY172
CASP195
CLYS200
CVAL260
CARG331
BCYS38
BHIS61
BCYS92
BCYS95
BCYS98
BCYS106
BCYS148
BGLY172
BASP195
BLYS200
BVAL260
BARG331
DCYS38
DHIS61
DCYS92
DCYS95
DCYS98
DCYS106
DCYS148
DGLY172
DASP195
DLYS200
DVAL260
DARG331
ACYS38
AHIS61
ACYS92
ACYS95
ACYS98
ACYS106
ACYS148
AGLY172

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PDB entries from 2024-05-15

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