1Q1N
APO AND HOLO STRUCTURES OF AN 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 | 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 | SER48 |
| A | HIS68 |
| A | CYS163 |
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 |
