2HSA
Crystal structure of 12-oxophytodienoate reductase 3 (OPR3) from tomato
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 | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 601 |
| Chain | Residue |
| A | ARG343 |
| A | TYR364 |
| A | ARG366 |
| A | HOH928 |
| B | ARG294 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 602 |
| Chain | Residue |
| A | GLY288 |
| B | ARG343 |
| B | TYR364 |
| B | ARG366 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL A 603 |
| Chain | Residue |
| A | LYS20 |
| A | PHE21 |
| A | ASP232 |
| A | HOH741 |
| A | HOH764 |
| site_id | AC4 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE FMN B 401 |
| Chain | Residue |
| A | GLY288 |
| A | GLN289 |
| A | GLU291 |
| 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 | HOH605 |
| B | HOH631 |
| site_id | AC5 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE FMN A 401 |
| Chain | Residue |
| A | ALA30 |
| A | PRO31 |
| A | MET32 |
| A | THR33 |
| A | GLY64 |
| A | GLN106 |
| A | HIS185 |
| A | HIS188 |
| A | ARG237 |
| A | SER319 |
| A | GLY320 |
| A | GLY321 |
| A | GLY342 |
| A | ARG343 |
| A | PHE369 |
| A | TYR370 |
| A | HOH613 |
| A | HOH624 |
| A | HOH645 |
| B | GLN289 |
| B | GLU291 |
| B | HOH613 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Region: {"description":"FMN"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16983071","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19660473","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
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) |
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 16983071 |
| Chain | Residue | Details |
| B | HIS185 | |
| B | TYR190 | |
| B | HIS188 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 16983071 |
| Chain | Residue | Details |
| A | HIS185 | |
| A | TYR190 | |
| A | HIS188 |
