1PS0
Crystal Structure of the NADP(H)-Dependent Cinnamyl Alcohol Dehydrogenase from Saccharomyces cerevisiae
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005575 | cellular_component | cellular_component |
A | 0005634 | cellular_component | nucleus |
A | 0005737 | cellular_component | cytoplasm |
A | 0006066 | biological_process | alcohol metabolic process |
A | 0006081 | biological_process | cellular aldehyde metabolic process |
A | 0008106 | molecular_function | alcohol dehydrogenase (NADP+) activity |
A | 0008270 | molecular_function | zinc ion binding |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
A | 0033833 | molecular_function | hydroxymethylfurfural reductase (NADH) activity |
A | 0033845 | molecular_function | hydroxymethylfurfural reductase (NADPH) activity |
A | 0033859 | biological_process | furaldehyde metabolic process |
A | 0045551 | molecular_function | cinnamyl-alcohol dehydrogenase activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0052675 | molecular_function | 3-methylbutanal reductase (NADPH) activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 1501 |
Chain | Residue |
A | CYS100 |
A | CYS103 |
A | CYS106 |
A | CYS114 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 1502 |
Chain | Residue |
A | CYS46 |
A | HIS68 |
A | CYS163 |
A | NAP4292 |
site_id | AC3 |
Number of Residues | 29 |
Details | BINDING SITE FOR RESIDUE NAP A 4292 |
Chain | Residue |
A | SER48 |
A | HIS51 |
A | TRP57 |
A | CYS163 |
A | THR167 |
A | GLY187 |
A | LEU188 |
A | GLY189 |
A | GLY190 |
A | ILE191 |
A | SER210 |
A | ARG211 |
A | LYS215 |
A | CYS250 |
A | ALA251 |
A | SER252 |
A | SER253 |
A | THR255 |
A | ASP256 |
A | ILE257 |
A | ILE275 |
A | ILE277 |
A | TYR298 |
A | SER299 |
A | ALA300 |
A | LEU301 |
A | ARG348 |
A | ZN1502 |
A | GLY47 |
Functional Information from PROSITE/UniProt
site_id | PS00059 |
Number of Residues | 15 |
Details | ADH_ZINC Zinc-containing alcohol dehydrogenases signature. GHEiVGKvvklGpkS |
Chain | Residue | Details |
A | GLY67-SER81 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15289102, ECO:0007744|PDB:1PIW, ECO:0007744|PDB:1Q1N |
Chain | Residue | Details |
A | CYS46 | |
A | HIS68 | |
A | CYS163 |
site_id | SWS_FT_FI2 |
Number of Residues | 11 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15289102, ECO:0007744|PDB:1PIW, ECO:0007744|PDB:1PS0 |
Chain | Residue | Details |
A | GLY47 | |
A | SER299 | |
A | LEU301 | |
A | GLY190 | |
A | ILE191 | |
A | SER210 | |
A | ARG211 | |
A | LYS215 | |
A | SER252 | |
A | THR255 | |
A | ILE277 |
site_id | SWS_FT_FI3 |
Number of Residues | 5 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15289102, ECO:0007744|PDB:1PIW |
Chain | Residue | Details |
A | HIS51 | |
A | LEU188 | |
A | CYS250 | |
A | TYR298 | |
A | ARG348 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15289102, ECO:0007744|PDB:1PIW, ECO:0007744|PDB:1PS0, ECO:0007744|PDB:1Q1N |
Chain | Residue | Details |
A | CYS100 | |
A | CYS103 | |
A | CYS106 | |
A | CYS114 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15289102, ECO:0007744|PDB:1PS0 |
Chain | Residue | Details |
A | ASP256 | |
A | ILE275 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956 |
Chain | Residue | Details |
A | SER131 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 |
Chain | Residue | Details |
A | SER359 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1guf |
Chain | Residue | Details |
A | TRP57 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1guf |
Chain | Residue | Details |
A | SER48 | |
A | HIS51 |