5DCU
Iridoid synthase from Catharanthus roseus - ternary complex with NADP+ and triethylene glycol carboxylic acid
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 | 32 |
Details | binding site for residue NAP A 900 |
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 | TEG902 |
A | HOH1003 |
A | HOH1017 |
A | HOH1026 |
A | HOH1032 |
A | HOH1045 |
A | HOH1054 |
A | GLY39 |
A | HOH1066 |
A | HOH1140 |
A | HOH1345 |
A | ILE40 |
A | ALA65 |
A | ARG66 |
A | ARG67 |
A | CYS83 |
A | ASP84 |
site_id | AC2 |
Number of Residues | 7 |
Details | binding site for residue EDO A 901 |
Chain | Residue |
A | HIS147 |
A | ARG171 |
A | GLU182 |
A | ARG200 |
A | HOH1004 |
A | HOH1027 |
A | HOH1072 |
site_id | AC3 |
Number of Residues | 8 |
Details | binding site for residue TEG A 902 |
Chain | Residue |
A | GLY144 |
A | ILE145 |
A | LYS146 |
A | TYR178 |
A | PRO201 |
A | ALA346 |
A | SER349 |
A | NAP900 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue EDO A 903 |
Chain | Residue |
A | ILE225 |
A | GLU229 |
A | MET313 |
A | LYS316 |
A | HOH1103 |
A | HOH1115 |
site_id | AC5 |
Number of Residues | 30 |
Details | binding site for residue NAP B 900 |
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 | TEG902 |
B | HOH1005 |
B | HOH1053 |
B | HOH1062 |
B | HOH1083 |
B | HOH1084 |
B | HOH1099 |
B | HOH1102 |
site_id | AC6 |
Number of Residues | 7 |
Details | binding site for residue EDO B 901 |
Chain | Residue |
B | HIS147 |
B | ARG171 |
B | GLU182 |
B | ARG200 |
B | HOH1008 |
B | HOH1052 |
B | HOH1054 |
site_id | AC7 |
Number of Residues | 8 |
Details | binding site for residue TEG B 902 |
Chain | Residue |
B | GLY144 |
B | ILE145 |
B | LYS146 |
B | TYR178 |
B | PRO201 |
B | ALA346 |
B | SER349 |
B | NAP900 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue EDO B 903 |
Chain | Residue |
B | MET313 |
B | LYS316 |
B | HOH1038 |
B | HOH1181 |
B | GLU229 |
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 |
B | TYR178 | |
A | 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 |
B | SER349 | |
A | SER349 |