5GQ0
Crystal structure of the Epithiospecifier Protein, ESP from Arabidopsis thaliana
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0009753 | biological_process | response to jasmonic acid |
| A | 0010150 | biological_process | leaf senescence |
| A | 0016829 | molecular_function | lyase activity |
| A | 0019762 | biological_process | glucosinolate catabolic process |
| A | 0030234 | molecular_function | enzyme regulator activity |
| A | 0042742 | biological_process | defense response to bacterium |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0080028 | biological_process | nitrile biosynthetic process |
| B | 0005515 | molecular_function | protein binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0009753 | biological_process | response to jasmonic acid |
| B | 0010150 | biological_process | leaf senescence |
| B | 0016829 | molecular_function | lyase activity |
| B | 0019762 | biological_process | glucosinolate catabolic process |
| B | 0030234 | molecular_function | enzyme regulator activity |
| B | 0042742 | biological_process | defense response to bacterium |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0080028 | biological_process | nitrile biosynthetic process |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:23999604, ECO:0000305|PubMed:27498030 |
| Chain | Residue | Details |
| B | ARG94 | |
| A | ARG94 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:27498030, ECO:0000305|PubMed:28479247 |
| Chain | Residue | Details |
| B | ARG157 | |
| A | ARG157 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:23999604, ECO:0000305|PubMed:27498030 |
| Chain | Residue | Details |
| B | LYS46 | |
| B | ARG94 | |
| B | PHE130 | |
| B | LYS211 | |
| A | LYS46 | |
| A | ARG94 | |
| A | PHE130 | |
| A | LYS211 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:28479247 |
| Chain | Residue | Details |
| B | THR129 | |
| A | THR129 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:27498030, ECO:0000305|PubMed:28479247 |
| Chain | Residue | Details |
| B | ARG157 | |
| A | ARG157 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:23999604, ECO:0000305|PubMed:27498030, ECO:0000305|PubMed:28479247 |
| Chain | Residue | Details |
| B | GLY186 | |
| A | ASP264 | |
| A | HIS268 | |
| A | TRP303 | |
| B | VAL244 | |
| B | GLU260 | |
| B | ASP264 | |
| B | HIS268 | |
| B | TRP303 | |
| A | GLY186 | |
| A | VAL244 | |
| A | GLU260 |
