5OR6
Crystal structures of PYR1/HAB1 in complex with synthetic analogues of Abscisic Acid
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004864 | molecular_function | protein phosphatase inhibitor activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005773 | cellular_component | vacuole |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0009705 | cellular_component | plant-type vacuole membrane |
| A | 0009738 | biological_process | abscisic acid-activated signaling pathway |
| A | 0010427 | molecular_function | abscisic acid binding |
| A | 0038023 | molecular_function | signaling receptor activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0044389 | molecular_function | ubiquitin-like protein ligase binding |
| A | 0062049 | cellular_component | protein phosphatase inhibitor complex |
| A | 0080163 | biological_process | regulation of protein serine/threonine phosphatase activity |
| A | 1902584 | biological_process | positive regulation of response to water deprivation |
| B | 0004722 | molecular_function | protein serine/threonine phosphatase activity |
| B | 0006470 | biological_process | protein dephosphorylation |
| B | 0043169 | molecular_function | cation binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | binding site for residue A4K A 201 |
| Chain | Residue |
| A | LYS59 |
| A | LEU117 |
| A | TYR120 |
| A | PHE159 |
| A | ALA160 |
| A | VAL163 |
| A | VAL164 |
| A | HOH303 |
| A | HOH307 |
| A | HOH315 |
| A | HOH349 |
| A | PHE61 |
| A | HOH355 |
| A | VAL83 |
| A | ALA89 |
| A | SER92 |
| A | GLU94 |
| A | PHE108 |
| A | ILE110 |
| A | HIS115 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue MN B 601 |
| Chain | Residue |
| B | ASP243 |
| B | ASP432 |
| B | ASP492 |
| B | MN602 |
| B | HOH712 |
| B | HOH720 |
| B | HOH737 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue MN B 602 |
| Chain | Residue |
| B | ASP243 |
| B | GLY244 |
| B | MN601 |
| B | HOH712 |
| B | HOH733 |
| B | HOH767 |
| B | HOH894 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue MN B 603 |
| Chain | Residue |
| B | ASP346 |
| B | ASP432 |
| B | HOH711 |
| B | HOH900 |
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: BINDING => ECO:0000269|PubMed:21658606, ECO:0007744|PDB:3NMT, ECO:0007744|PDB:3QN1, ECO:0007744|PDB:3RT0, ECO:0007744|PDB:3UJG, ECO:0007744|PDB:3ZVU, ECO:0007744|PDB:4LA7, ECO:0007744|PDB:4LG5, ECO:0007744|PDB:4LGA, ECO:0007744|PDB:4WVO |
| Chain | Residue | Details |
| B | ASP243 | |
| B | ASP432 | |
| B | ASP492 | |
| A | GLU141 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19898420, ECO:0007744|PDB:3KB3 |
| Chain | Residue | Details |
| B | GLY244 | |
| A | SER152 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | SITE: Lock |
| Chain | Residue | Details |
| B | TRP385 |
