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 | 0009507 | cellular_component | chloroplast |
| 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 | 0009507 | cellular_component | chloroplast |
| 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 | 96 |
| Details | Repeat: {"description":"Kelch 1","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 92 |
| Details | Repeat: {"description":"Kelch 2","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 110 |
| Details | Repeat: {"description":"Kelch 3","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"23999604","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"27498030","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"27498030","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"28479247","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"23999604","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"27498030","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"28479247","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"27498030","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"28479247","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"23999604","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"27498030","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"28479247","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 46 |
| Details | Repeat: {"description":"Kelch 4","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
