3UJG
Crystal structure of SnRK2.6 in complex with HAB1
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0004674 | molecular_function | protein serine/threonine kinase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0005985 | biological_process | sucrose metabolic process |
| A | 0006468 | biological_process | protein phosphorylation |
| A | 0006636 | biological_process | unsaturated fatty acid biosynthetic process |
| A | 0006952 | biological_process | defense response |
| A | 0006970 | biological_process | response to osmotic stress |
| A | 0009414 | biological_process | response to water deprivation |
| A | 0009651 | biological_process | response to salt stress |
| A | 0009737 | biological_process | response to abscisic acid |
| A | 0009738 | biological_process | abscisic acid-activated signaling pathway |
| A | 0009789 | biological_process | positive regulation of abscisic acid-activated signaling pathway |
| A | 0009931 | molecular_function | calcium-dependent protein serine/threonine kinase activity |
| A | 0010118 | biological_process | stomatal movement |
| A | 0010119 | biological_process | regulation of stomatal movement |
| A | 0010359 | biological_process | regulation of anion channel activity |
| A | 0016301 | molecular_function | kinase activity |
| A | 0019432 | biological_process | triglyceride biosynthetic process |
| A | 0019903 | molecular_function | protein phosphatase binding |
| A | 0042742 | biological_process | defense response to bacterium |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046777 | biological_process | protein autophosphorylation |
| A | 0048366 | biological_process | leaf development |
| A | 0071244 | biological_process | cellular response to carbon dioxide |
| A | 0071485 | biological_process | cellular response to absence of light |
| A | 0090333 | biological_process | regulation of stomatal closure |
| A | 0106310 | molecular_function | protein serine kinase activity |
| A | 1902456 | biological_process | regulation of stomatal opening |
| A | 2000377 | biological_process | regulation of reactive oxygen species metabolic process |
| 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 | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 363 |
| Chain | Residue |
| A | ARG139 |
| A | LYS142 |
| B | GLN384 |
| B | TRP385 |
| B | GLN386 |
| B | GLY387 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 364 |
| Chain | Residue |
| B | ARG199 |
| B | GLY244 |
| B | HIS245 |
| A | LYS174 |
| A | SER175 |
| A | THR176 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 100 |
| Chain | Residue |
| B | ASP204 |
| B | ASP243 |
| B | GLY244 |
| B | MG512 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 512 |
| Chain | Residue |
| B | MG100 |
| B | ASP243 |
| B | ASP432 |
| B | ASP492 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 513 |
| Chain | Residue |
| A | LYS174 |
| B | ARG199 |
| B | SER200 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 24 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGSGNFGVARlMrdkqsnel..........VAVK |
| Chain | Residue | Details |
| A | ILE27-LYS50 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VcHrDLKleNTLL |
| Chain | Residue | Details |
| A | VAL136-LEU148 |
| 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 |
| 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 | LYS50 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | SITE: Lock |
| Chain | Residue | Details |
| B | TRP385 | |
| A | SER29 | |
| A | SER43 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:16766677 |
| Chain | Residue | Details |
| A | SER175 |
