5COA
Crystal structure of iridoid synthase at 2.2-angstrom resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006629 | biological_process | lipid metabolic process |
| 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 | 0006629 | biological_process | lipid metabolic process |
| 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 | 7 |
| Details | binding site for residue P6G A 2001 |
| Chain | Residue |
| A | GLU113 |
| A | LYS146 |
| A | VAL174 |
| A | ASN176 |
| A | PHE177 |
| A | TYR178 |
| A | HOH2109 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 2002 |
| Chain | Residue |
| A | ARG67 |
| A | THR38 |
| A | ARG66 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 2003 |
| Chain | Residue |
| A | CYS244 |
| A | TYR245 |
| B | CYS244 |
| B | TYR245 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 B 401 |
| Chain | Residue |
| B | THR38 |
| B | ALA65 |
| B | ARG66 |
| B | ARG67 |
| B | HOH618 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 B 402 |
| Chain | Residue |
| B | ALA310 |
| B | ALA338 |
| B | ALA339 |
| B | PHE340 |
| B | TRP341 |
| B | HOH503 |
| B | HOH584 |
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 | GLN142 | |
| A | VAL204 | |
| A | SER211 | |
| B | THR38 | |
| B | ARG66 | |
| B | ASP84 | |
| B | SER108 | |
| B | GLN142 | |
| B | VAL204 | |
| B | SER211 | |
| A | THR38 | |
| A | ARG66 | |
| A | ASP84 | |
| A | SER108 |
| 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 |
