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 | 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 |
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) |