5DBF
Crystal Structure of Iridoid Synthase from Cantharanthus roseus in complex with NADPH
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0016099 | biological_process | monoterpenoid biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| A | 0016628 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0016099 | biological_process | monoterpenoid biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| B | 0016628 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 24 |
| Details | binding site for residue NDP A 401 |
| Chain | Residue |
| A | GLY36 |
| A | VAL85 |
| A | SER108 |
| A | TRP109 |
| A | MET121 |
| A | GLN142 |
| A | THR143 |
| A | TYR178 |
| A | PRO201 |
| A | ALA202 |
| A | VAL204 |
| A | THR38 |
| A | SER211 |
| A | MET212 |
| A | MET213 |
| A | HOH516 |
| A | HOH535 |
| A | GLY39 |
| A | ILE40 |
| A | ALA65 |
| A | ARG66 |
| A | ARG67 |
| A | CYS83 |
| A | ASP84 |
| site_id | AC2 |
| Number of Residues | 25 |
| Details | binding site for residue NDP B 401 |
| Chain | Residue |
| B | GLY36 |
| B | THR38 |
| B | GLY39 |
| B | ILE40 |
| B | ALA65 |
| B | ARG66 |
| B | ARG67 |
| B | CYS83 |
| B | ASP84 |
| B | VAL85 |
| B | SER108 |
| B | TRP109 |
| B | MET121 |
| B | GLN142 |
| B | THR143 |
| B | TYR178 |
| B | PRO201 |
| B | ALA202 |
| B | VAL204 |
| B | SER211 |
| B | MET212 |
| B | MET213 |
| B | HOH511 |
| B | HOH552 |
| B | HOH569 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: ACT_SITE => ECO:0000269|PubMed:26768532 |
| Chain | Residue | Details |
| A | LYS146 | |
| A | TYR178 | |
| B | LYS146 | |
| B | TYR178 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:26551396, ECO:0000269|PubMed:26768532, ECO:0000269|PubMed:26868105, ECO:0007744|PDB:5COB, ECO:0007744|PDB:5DBF, ECO:0007744|PDB:5DF1 |
| Chain | Residue | Details |
| A | THR38 | |
| B | ASP84 | |
| B | SER108 | |
| B | GLN142 | |
| B | VAL204 | |
| B | SER211 | |
| A | ARG66 | |
| A | ASP84 | |
| A | SER108 | |
| A | GLN142 | |
| A | VAL204 | |
| A | SER211 | |
| B | THR38 | |
| B | ARG66 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:26768532, ECO:0007744|PDB:5DBI |
| Chain | Residue | Details |
| A | LYS146 | |
| B | LYS146 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:26768532, ECO:0000269|PubMed:26868105, ECO:0007744|PDB:5COB, ECO:0007744|PDB:5DBI |
| Chain | Residue | Details |
| A | TYR178 | |
| B | TYR178 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:26768532, ECO:0000269|PubMed:26868105, ECO:0007744|PDB:5COB |
| Chain | Residue | Details |
| A | SER349 | |
| B | SER349 |
