3K3K
Crystal structure of dimeric abscisic acid (ABA) receptor pyrabactin resistance 1 (PYR1) with ABA-bound closed-lid and ABA-free open-lid subunits
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 | 0019207 | molecular_function | kinase regulator activity |
| 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 | 1902584 | biological_process | positive regulation of response to water deprivation |
| B | 0004864 | molecular_function | protein phosphatase inhibitor activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005773 | cellular_component | vacuole |
| B | 0005829 | cellular_component | cytosol |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0009705 | cellular_component | plant-type vacuole membrane |
| B | 0009738 | biological_process | abscisic acid-activated signaling pathway |
| B | 0010427 | molecular_function | abscisic acid binding |
| B | 0019207 | molecular_function | kinase regulator activity |
| B | 0038023 | molecular_function | signaling receptor activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0044389 | molecular_function | ubiquitin-like protein ligase binding |
| B | 0062049 | cellular_component | protein phosphatase inhibitor complex |
| B | 1902584 | biological_process | positive regulation of response to water deprivation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE A8S B 1001 |
| Chain | Residue |
| B | LYS59 |
| B | PHE159 |
| B | VAL163 |
| B | HOH200 |
| B | HOH214 |
| B | HOH220 |
| B | HOH221 |
| B | HOH297 |
| B | VAL83 |
| B | PRO88 |
| B | ALA89 |
| B | SER92 |
| B | PHE108 |
| B | ILE110 |
| B | LEU117 |
| B | TYR120 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 306 |
| Details | Region: {"description":"START-like"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Motif: {"description":"Gate loop","evidences":[{"source":"UniProtKB","id":"Q8VZS8","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Motif: {"description":"Latch loop","evidences":[{"source":"UniProtKB","id":"Q8VZS8","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 26 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19898494","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19933100","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Site: {"description":"Involved in interactions with PP2Cs","evidences":[{"source":"PubMed","id":"19407142","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine; by CARK1","evidences":[{"source":"PubMed","id":"29928509","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
