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1Q1N

APO AND HOLO STRUCTURES OF AN 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_processaldehyde 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
ASER48
AHIS68
ACYS163

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 site: {"evidences":[{"source":"PubMed","id":"15289102","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1PIW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Q1N","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues11
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15289102","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1PIW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PS0","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15289102","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1PIW","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15289102","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1PIW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1PS0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Q1N","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15289102","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1PS0","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

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

243083

PDB entries from 2025-10-15

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