5UR6
PYR1 bound to the rationally designed agonist cyanabactin
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 201 |
| Chain | Residue |
| A | GLN36 |
| A | GLN169 |
| A | ARG180 |
| A | ASN181 |
| A | HOH323 |
| A | HOH399 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 A 202 |
| Chain | Residue |
| A | ARG50 |
| A | HOH353 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 203 |
| Chain | Residue |
| A | ARG51 |
| A | LYS54 |
| A | HOH303 |
| A | HOH361 |
| A | HOH385 |
| A | SER47 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 204 |
| Chain | Residue |
| A | ARG104 |
| A | ARG128 |
| A | HOH384 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | binding site for residue SO4 A 205 |
| Chain | Residue |
| A | GLU4 |
| A | ARG37 |
| A | HIS39 |
| A | HIS39 |
| A | ARG134 |
| A | TRP136 |
| A | HOH315 |
| A | HOH338 |
| A | HOH347 |
| A | HOH395 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 A 206 |
| Chain | Residue |
| A | GLU102 |
| A | GLU102 |
| A | ARG103 |
| A | ARG103 |
| A | HOH302 |
| A | HOH302 |
| A | HOH383 |
| site_id | AC7 |
| Number of Residues | 13 |
| Details | binding site for residue 8KM A 207 |
| Chain | Residue |
| A | PHE61 |
| A | ILE62 |
| A | VAL81 |
| A | VAL83 |
| A | ALA89 |
| A | SER92 |
| A | GLU94 |
| A | PHE108 |
| A | LEU117 |
| A | TYR120 |
| A | PHE159 |
| A | HOH344 |
| A | HOH364 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Motif: {"description":"Gate loop","evidences":[{"source":"UniProtKB","id":"Q8VZS8","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Motif: {"description":"Latch loop","evidences":[{"source":"UniProtKB","id":"Q8VZS8","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 13 |
| 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_FI4 |
| Number of Residues | 1 |
| Details | Site: {"description":"Involved in interactions with PP2Cs","evidences":[{"source":"PubMed","id":"19407142","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine; by CARK1","evidences":[{"source":"PubMed","id":"29928509","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
