9H0H
X-RAY CRYSTAL STRUCTURE OF THE CsPYL1-OPABACTIN-HAB1 TERNARY COMPLEX
This is a non-PDB format compatible entry.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004864 | molecular_function | protein phosphatase inhibitor activity |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0009738 | biological_process | abscisic acid-activated signaling pathway |
| A | 0010427 | molecular_function | abscisic acid binding |
| A | 0038023 | molecular_function | signaling receptor activity |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0062049 | cellular_component | protein phosphatase inhibitor complex |
Functional Information from PROSITE/UniProt
| site_id | PS01032 |
| Number of Residues | 9 |
| Details | PPM_1 PPM-type phosphatase domain signature. FFGVYDGHG |
| Chain | Residue | Details |
| B | PHE238-GLY246 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21658606","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3NMT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3QN1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3RT0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3UJG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ZVU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4LA7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4LG5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4LGA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4WVO","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19898420","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3KB3","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Site: {"description":"Lock"} |
| Chain | Residue | Details |
