5COB
Crystal structure of iridoid synthase in complex with NADP+ and 8-oxogeranial at 2.65-angstrom resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005829 | cellular_component | cytosol |
| A | 0006720 | biological_process | isoprenoid metabolic process |
| A | 0016099 | biological_process | monoterpenoid biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| 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 | 0005829 | cellular_component | cytosol |
| B | 0006720 | biological_process | isoprenoid metabolic process |
| B | 0016099 | biological_process | monoterpenoid biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| 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 |
| C | 0005829 | cellular_component | cytosol |
| C | 0006720 | biological_process | isoprenoid metabolic process |
| C | 0016099 | biological_process | monoterpenoid biosynthetic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016628 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0042803 | molecular_function | protein homodimerization activity |
| D | 0005829 | cellular_component | cytosol |
| D | 0006720 | biological_process | isoprenoid metabolic process |
| D | 0016099 | biological_process | monoterpenoid biosynthetic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016628 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0042803 | molecular_function | protein homodimerization activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 30 |
| Details | binding site for residue NAP A 1001 |
| Chain | Residue |
| A | GLY36 |
| A | VAL85 |
| A | VAL107 |
| A | SER108 |
| A | TRP109 |
| A | ILE110 |
| A | GLN142 |
| A | THR143 |
| A | TYR178 |
| A | PRO201 |
| A | ALA202 |
| A | THR38 |
| A | VAL204 |
| A | SER211 |
| A | MET212 |
| A | MET213 |
| A | XOG1002 |
| A | PG41003 |
| A | HOH1102 |
| A | HOH1107 |
| A | HOH1108 |
| A | HOH1128 |
| A | GLY39 |
| A | HOH1129 |
| A | ILE40 |
| A | ALA65 |
| A | ARG66 |
| A | ARG67 |
| A | CYS83 |
| A | ASP84 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | binding site for residue XOG A 1002 |
| Chain | Residue |
| A | GLY144 |
| A | ILE145 |
| A | LYS146 |
| A | PHE149 |
| A | TYR178 |
| A | MET213 |
| A | PHE342 |
| A | ILE345 |
| A | ALA346 |
| A | SER349 |
| A | NAP1001 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue PG4 A 1003 |
| Chain | Residue |
| A | LYS146 |
| A | GLY150 |
| A | PHE152 |
| A | ASN176 |
| A | PHE177 |
| A | TYR178 |
| A | NAP1001 |
| site_id | AC4 |
| Number of Residues | 27 |
| Details | binding site for residue NAP B 1001 |
| Chain | Residue |
| B | GLY36 |
| B | THR38 |
| B | GLY39 |
| B | ILE40 |
| B | ALA65 |
| B | ARG66 |
| B | ARG67 |
| B | CYS83 |
| B | ASP84 |
| B | VAL85 |
| B | VAL107 |
| B | SER108 |
| B | TRP109 |
| B | GLN142 |
| B | THR143 |
| B | TYR178 |
| B | PRO201 |
| B | ALA202 |
| B | VAL204 |
| B | SER211 |
| B | MET212 |
| B | MET213 |
| B | XOG1002 |
| B | PG41003 |
| B | HOH1104 |
| B | HOH1117 |
| B | HOH1132 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | binding site for residue XOG B 1002 |
| Chain | Residue |
| B | GLY144 |
| B | ILE145 |
| B | LYS146 |
| B | PHE149 |
| B | TYR178 |
| B | MET213 |
| B | PHE342 |
| B | ILE345 |
| B | ALA346 |
| B | SER349 |
| B | NAP1001 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue PG4 B 1003 |
| Chain | Residue |
| B | GLU113 |
| B | LYS146 |
| B | GLY150 |
| B | PHE152 |
| B | ASN176 |
| B | PHE177 |
| B | TYR178 |
| B | NAP1001 |
| site_id | AC7 |
| Number of Residues | 28 |
| Details | binding site for residue NAP C 1001 |
| Chain | Residue |
| C | ARG66 |
| C | ARG67 |
| C | CYS83 |
| C | ASP84 |
| C | VAL85 |
| C | VAL107 |
| C | SER108 |
| C | TRP109 |
| C | GLN142 |
| C | THR143 |
| C | PHE177 |
| C | TYR178 |
| C | PRO201 |
| C | ALA202 |
| C | VAL204 |
| C | SER211 |
| C | MET212 |
| C | MET213 |
| C | XOG1002 |
| C | PG41003 |
| C | HOH1102 |
| C | HOH1108 |
| C | HOH1119 |
| C | GLY36 |
| C | THR38 |
| C | GLY39 |
| C | ILE40 |
| C | ALA65 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | binding site for residue XOG C 1002 |
| Chain | Residue |
| C | GLY144 |
| C | ILE145 |
| C | LYS146 |
| C | PHE149 |
| C | TYR178 |
| C | MET213 |
| C | PHE342 |
| C | ILE345 |
| C | SER349 |
| C | NAP1001 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | binding site for residue PG4 C 1003 |
| Chain | Residue |
| C | GLU113 |
| C | LYS146 |
| C | GLY150 |
| C | PHE152 |
| C | ASN176 |
| C | PHE177 |
| C | TYR178 |
| C | MET213 |
| C | NAP1001 |
| site_id | AD1 |
| Number of Residues | 27 |
| Details | binding site for residue NAP D 1001 |
| Chain | Residue |
| D | GLY36 |
| D | THR38 |
| D | GLY39 |
| D | ILE40 |
| D | ALA65 |
| D | ARG66 |
| D | ARG67 |
| D | CYS83 |
| D | ASP84 |
| D | VAL85 |
| D | VAL107 |
| D | SER108 |
| D | TRP109 |
| D | GLN142 |
| D | THR143 |
| D | TYR178 |
| D | PRO201 |
| D | ALA202 |
| D | VAL204 |
| D | SER211 |
| D | MET212 |
| D | MET213 |
| D | XOG1002 |
| D | PG41003 |
| D | HOH1101 |
| D | HOH1114 |
| D | HOH1119 |
| site_id | AD2 |
| Number of Residues | 10 |
| Details | binding site for residue XOG D 1002 |
| Chain | Residue |
| D | GLY144 |
| D | ILE145 |
| D | LYS146 |
| D | PHE149 |
| D | TYR178 |
| D | MET213 |
| D | ILE345 |
| D | ALA346 |
| D | SER349 |
| D | NAP1001 |
| site_id | AD3 |
| Number of Residues | 10 |
| Details | binding site for residue PG4 D 1003 |
| Chain | Residue |
| D | TRP109 |
| D | GLU113 |
| D | LYS146 |
| D | GLY150 |
| D | PHE152 |
| D | ASN176 |
| D | PHE177 |
| D | TYR178 |
| D | MET213 |
| D | NAP1001 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"26768532","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 36 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26551396","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26768532","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26868105","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5COB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5DBF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5DF1","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26768532","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5DBI","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26768532","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26868105","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5COB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5DBI","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26768532","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26868105","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5COB","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
