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1PS0

Crystal Structure of the NADP(H)-Dependent Cinnamyl Alcohol Dehydrogenase from Saccharomyces cerevisiae

Functional Information from GO Data
ChainGOidnamespacecontents
A0005575cellular_componentcellular_component
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0006066biological_processalcohol metabolic process
A0006081biological_processcellular aldehyde metabolic process
A0008106molecular_functionalcohol dehydrogenase (NADP+) activity
A0008270molecular_functionzinc ion binding
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0033833molecular_functionhydroxymethylfurfural reductase (NADH) activity
A0033845molecular_functionhydroxymethylfurfural reductase (NADPH) activity
A0033859biological_processfuraldehyde metabolic process
A0045551molecular_functioncinnamyl-alcohol dehydrogenase activity
A0046872molecular_functionmetal ion binding
A0052675molecular_function3-methylbutanal reductase (NADPH) activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1501
ChainResidue
ACYS100
ACYS103
ACYS106
ACYS114

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1502
ChainResidue
ACYS46
AHIS68
ACYS163
ANAP4292

site_idAC3
Number of Residues29
DetailsBINDING SITE FOR RESIDUE NAP A 4292
ChainResidue
ASER48
AHIS51
ATRP57
ACYS163
ATHR167
AGLY187
ALEU188
AGLY189
AGLY190
AILE191
ASER210
AARG211
ALYS215
ACYS250
AALA251
ASER252
ASER253
ATHR255
AASP256
AILE257
AILE275
AILE277
ATYR298
ASER299
AALA300
ALEU301
AARG348
AZN1502
AGLY47

Functional Information from PROSITE/UniProt
site_idPS00059
Number of Residues15
DetailsADH_ZINC Zinc-containing alcohol dehydrogenases signature. GHEiVGKvvklGpkS
ChainResidueDetails
AGLY67-SER81

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:15289102, ECO:0007744|PDB:1PIW, ECO:0007744|PDB:1Q1N
ChainResidueDetails
ACYS46
AHIS68
ACYS163

site_idSWS_FT_FI2
Number of Residues11
DetailsBINDING: BINDING => ECO:0000269|PubMed:15289102, ECO:0007744|PDB:1PIW, ECO:0007744|PDB:1PS0
ChainResidueDetails
AGLY47
ASER299
ALEU301
AGLY190
AILE191
ASER210
AARG211
ALYS215
ASER252
ATHR255
AILE277

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:15289102, ECO:0007744|PDB:1PIW
ChainResidueDetails
AHIS51
ALEU188
ACYS250
ATYR298
AARG348

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:15289102, ECO:0007744|PDB:1PIW, ECO:0007744|PDB:1PS0, ECO:0007744|PDB:1Q1N
ChainResidueDetails
ACYS100
ACYS103
ACYS106
ACYS114

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:15289102, ECO:0007744|PDB:1PS0
ChainResidueDetails
AASP256
AILE275

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956
ChainResidueDetails
ASER131

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
ChainResidueDetails
ASER359

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1guf
ChainResidueDetails
ATRP57

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1guf
ChainResidueDetails
ASER48
AHIS51

219140

PDB entries from 2024-05-01

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