5DCY
Iridoid synthase G150A mutant from Catharanthus roseus - binary complex with NADP+
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 | 31 |
Details | binding site for residue NAP A 900 |
Chain | Residue |
A | GLY36 |
A | VAL85 |
A | SER86 |
A | SER108 |
A | TRP109 |
A | MET121 |
A | GLN142 |
A | THR143 |
A | TYR178 |
A | PRO201 |
A | ALA202 |
A | THR38 |
A | VAL204 |
A | SER211 |
A | MET212 |
A | MET213 |
A | PGE901 |
A | HOH1020 |
A | HOH1036 |
A | HOH1065 |
A | HOH1073 |
A | HOH1083 |
A | GLY39 |
A | HOH1143 |
A | HOH1241 |
A | ILE40 |
A | ALA65 |
A | ARG66 |
A | ARG67 |
A | CYS83 |
A | ASP84 |
site_id | AC2 |
Number of Residues | 9 |
Details | binding site for residue PGE A 901 |
Chain | Residue |
A | GLU113 |
A | LYS146 |
A | ILE151 |
A | ASN176 |
A | PHE177 |
A | TYR178 |
A | MET213 |
A | ILE345 |
A | NAP900 |
site_id | AC3 |
Number of Residues | 7 |
Details | binding site for residue EDO A 902 |
Chain | Residue |
A | HIS147 |
A | ARG171 |
A | GLU182 |
A | ARG200 |
A | HOH1003 |
A | HOH1051 |
A | HOH1101 |
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 | HOH1121 |
A | HOH1151 |
site_id | AC5 |
Number of Residues | 32 |
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 | PGE901 |
B | HOH1001 |
B | HOH1008 |
B | HOH1037 |
B | HOH1040 |
B | HOH1043 |
B | HOH1049 |
B | HOH1085 |
B | HOH1173 |
B | HOH1220 |
site_id | AC6 |
Number of Residues | 7 |
Details | binding site for residue PGE B 901 |
Chain | Residue |
B | GLU113 |
B | LYS146 |
B | ASN176 |
B | PHE177 |
B | TYR178 |
B | MET213 |
B | NAP900 |
site_id | AC7 |
Number of Residues | 8 |
Details | binding site for residue EDO B 902 |
Chain | Residue |
B | HOH1252 |
B | ALA310 |
B | ALA338 |
B | ALA339 |
B | PHE340 |
B | TRP341 |
B | HOH1077 |
B | HOH1152 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue EDO B 903 |
Chain | Residue |
B | ILE225 |
B | CYS226 |
B | GLU229 |
B | MET313 |
B | HOH1036 |
B | HOH1059 |
site_id | AC9 |
Number of Residues | 7 |
Details | binding site for residue EDO B 904 |
Chain | Residue |
B | HIS147 |
B | ARG171 |
B | GLU182 |
B | ARG200 |
B | HOH1004 |
B | HOH1050 |
B | HOH1069 |
site_id | AD1 |
Number of Residues | 3 |
Details | binding site for residue EDO B 905 |
Chain | Residue |
B | ASP250 |
B | ASP252 |
B | ARG368 |
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 |