3HGS
Crystal structure of tomato OPR3 in complex with pHB
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005777 | cellular_component | peroxisome |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006631 | biological_process | fatty acid metabolic process |
| A | 0006633 | biological_process | fatty acid biosynthetic process |
| A | 0009695 | biological_process | jasmonic acid biosynthetic process |
| A | 0010181 | molecular_function | FMN binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016629 | molecular_function | 12-oxophytodienoate reductase activity |
| A | 0031408 | biological_process | oxylipin biosynthetic process |
| A | 0042802 | molecular_function | identical protein binding |
| B | 0005777 | cellular_component | peroxisome |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0006631 | biological_process | fatty acid metabolic process |
| B | 0006633 | biological_process | fatty acid biosynthetic process |
| B | 0009695 | biological_process | jasmonic acid biosynthetic process |
| B | 0010181 | molecular_function | FMN binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016629 | molecular_function | 12-oxophytodienoate reductase activity |
| B | 0031408 | biological_process | oxylipin biosynthetic process |
| B | 0042802 | molecular_function | identical protein binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE FMN A 401 |
| Chain | Residue |
| A | ALA30 |
| A | THR280 |
| A | SER319 |
| A | GLY320 |
| A | GLY321 |
| A | GLY342 |
| A | ARG343 |
| A | PHE369 |
| A | TYR370 |
| A | PHB402 |
| A | HOH436 |
| A | PRO31 |
| A | HOH447 |
| A | HOH450 |
| A | MET32 |
| A | THR33 |
| A | GLY64 |
| A | GLN106 |
| A | HIS185 |
| A | HIS188 |
| A | ARG237 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PHB A 402 |
| Chain | Residue |
| A | THR33 |
| A | PHE74 |
| A | TRP108 |
| A | HIS185 |
| A | HIS188 |
| A | TYR190 |
| A | TYR370 |
| A | FMN401 |
| site_id | AC3 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE FMN B 401 |
| Chain | Residue |
| B | ALA30 |
| B | PRO31 |
| B | MET32 |
| B | THR33 |
| B | GLY64 |
| B | GLN106 |
| B | HIS185 |
| B | HIS188 |
| B | ARG237 |
| B | SER319 |
| B | GLY320 |
| B | GLY321 |
| B | GLY342 |
| B | ARG343 |
| B | PHE369 |
| B | TYR370 |
| B | PHB402 |
| B | HOH455 |
| B | HOH477 |
| B | HOH485 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PHB B 402 |
| Chain | Residue |
| B | PHE74 |
| B | TRP108 |
| B | HIS185 |
| B | HIS188 |
| B | TYR190 |
| B | TYR370 |
| B | FMN401 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000250 |
| Chain | Residue | Details |
| A | TYR190 | |
| B | TYR190 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16983071, ECO:0000269|PubMed:19660473 |
| Chain | Residue | Details |
| A | PRO31 | |
| B | GLY321 | |
| A | GLY64 | |
| A | GLN106 | |
| A | ARG237 | |
| A | GLY321 | |
| B | PRO31 | |
| B | GLY64 | |
| B | GLN106 | |
| B | ARG237 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | HIS185 | |
| A | ARG283 | |
| A | GLY342 | |
| B | HIS185 | |
| B | ARG283 | |
| B | GLY342 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 697 |
| Chain | Residue | Details |
| A | HIS185 | electrostatic stabiliser |
| A | HIS188 | electrostatic stabiliser |
| A | TYR190 | proton shuttle (general acid/base) |
| site_id | MCSA2 |
| Number of Residues | 3 |
| Details | M-CSA 697 |
| Chain | Residue | Details |
| B | HIS185 | electrostatic stabiliser |
| B | HIS188 | electrostatic stabiliser |
| B | TYR190 | proton shuttle (general acid/base) |
