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1HDX

THREE-DIMENSIONAL STRUCTURES OF THREE HUMAN ALCOHOL DEHYDROGENASE VARIANTS: CORRELATIONS WITH THEIR FUNCTIONAL DIFFERENCES

Functional Information from GO Data
ChainGOidnamespacecontents
A0001523biological_processretinoid metabolic process
A0004022molecular_functionalcohol dehydrogenase (NAD+) activity
A0004745molecular_functionall-trans-retinol dehydrogenase (NAD+) activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006629biological_processlipid metabolic process
A0008270molecular_functionzinc ion binding
A0016491molecular_functionoxidoreductase activity
A0042572biological_processretinol metabolic process
A0042573biological_processretinoic acid metabolic process
A0046872molecular_functionmetal ion binding
B0001523biological_processretinoid metabolic process
B0004022molecular_functionalcohol dehydrogenase (NAD+) activity
B0004745molecular_functionall-trans-retinol dehydrogenase (NAD+) activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006629biological_processlipid metabolic process
B0008270molecular_functionzinc ion binding
B0016491molecular_functionoxidoreductase activity
B0042572biological_processretinol metabolic process
B0042573biological_processretinoic acid metabolic process
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 375
ChainResidue
ACYS97
ACYS100
ACYS103
ACYS111

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN A 376
ChainResidue
ACYS46
AHIS67
ACYS174

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 375
ChainResidue
BCYS97
BCYS100
BCYS103
BCYS111

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 376
ChainResidue
BCYS46
BTHR48
BHIS67
BCYS174
BNAD377

site_idAC5
Number of Residues23
DetailsBINDING SITE FOR RESIDUE NAD A 377
ChainResidue
AARG47
ATHR48
AHIS51
ACYS174
ATHR178
AGLY199
ALEU200
AGLY201
AGLY202
AVAL203
AASP223
ALYS228
AILE269
AARG271
AVAL292
AGLY293
AVAL294
AALA317
ATYR319
AARG369
AHOH383
AHOH384
AHOH385

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CXL A 378
ChainResidue
ALEU57
APHE93
ALEU116

site_idAC7
Number of Residues26
DetailsBINDING SITE FOR RESIDUE NAD B 377
ChainResidue
BARG47
BTHR48
BHIS51
BCYS174
BTHR178
BGLY199
BLEU200
BGLY201
BGLY202
BVAL203
BASP223
BLYS228
BVAL268
BILE269
BARG271
BVAL292
BGLY293
BVAL294
BALA317
BTYR319
BARG369
BZN376
BHOH606
BHOH607
BHOH609
BHOH638

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CXL B 378
ChainResidue
AMET306
BLEU116
BVAL318

site_idCAL
Number of Residues1
Details
ChainResidue
ACXL378

site_idCBL
Number of Residues1
Details
ChainResidue
BCXL378

site_idNAD
Number of Residues1
Details
ChainResidue
ANAD377

site_idNBD
Number of Residues1
Details
ChainResidue
BNAD377

site_idZA1
Number of Residues4
Details
ChainResidue
ACYS46
AHIS67
ACYS174
AZN376

site_idZA2
Number of Residues5
Details
ChainResidue
ACYS97
ACYS100
ACYS103
ACYS111
AZN375

site_idZB1
Number of Residues4
Details
ChainResidue
BCYS46
BHIS67
BCYS174
BZN376

site_idZB2
Number of Residues5
Details
ChainResidue
BCYS97
BCYS100
BCYS103
BCYS111
BZN375

Functional Information from PROSITE/UniProt
site_idPS00059
Number of Residues15
DetailsADH_ZINC Zinc-containing alcohol dehydrogenases signature. GHEaAGIvesvGegV
ChainResidueDetails
AGLY66-VAL80

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues34
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsModified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"6391920","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1teh
ChainResidueDetails
ATHR48
AARG47

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1teh
ChainResidueDetails
BTHR48
BARG47

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1teh
ChainResidueDetails
ALEU57

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1teh
ChainResidueDetails
BLEU57

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1teh
ChainResidueDetails
ATHR48
AHIS51

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1teh
ChainResidueDetails
BTHR48
BHIS51

247536

PDB entries from 2026-01-14

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