6J5U
Ligand-triggered allosteric ADP release primes a plant NLR complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006952 | biological_process | defense response |
| A | 0016020 | cellular_component | membrane |
| A | 0042742 | biological_process | defense response to bacterium |
| A | 0043531 | molecular_function | ADP binding |
| A | 0050776 | biological_process | regulation of immune response |
| A | 0050829 | biological_process | defense response to Gram-negative bacterium |
| A | 0051707 | biological_process | response to other organism |
| A | 0098542 | biological_process | defense response to other organism |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004672 | molecular_function | protein kinase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006468 | biological_process | protein phosphorylation |
| B | 0006952 | biological_process | defense response |
| B | 0007166 | biological_process | cell surface receptor signaling pathway |
| B | 0009266 | biological_process | response to temperature stimulus |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0042742 | biological_process | defense response to bacterium |
| B | 1900426 | biological_process | positive regulation of defense response to bacterium |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0004672 | molecular_function | protein kinase activity |
| C | 0004674 | molecular_function | protein serine/threonine kinase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005634 | cellular_component | nucleus |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0006468 | biological_process | protein phosphorylation |
| C | 0006952 | biological_process | defense response |
| C | 0009507 | cellular_component | chloroplast |
| C | 0016020 | cellular_component | membrane |
| C | 0016301 | molecular_function | kinase activity |
| C | 0016740 | molecular_function | transferase activity |
| C | 0030957 | molecular_function | Tat protein binding |
| C | 0106310 | molecular_function | protein serine kinase activity |
| C | 1900426 | biological_process | positive regulation of defense response to bacterium |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 33 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGGFGCVFkGwidqtsltasrpgsgiv.VAVK |
| Chain | Residue | Details |
| C | LEU92-LYS124 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ViYrDFKaaNILL |
| Chain | Residue | Details |
| C | VAL215-LEU227 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 23 |
| Details | Repeat: {"description":"LRR 1","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | Repeat: {"description":"LRR 2","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 24 |
| Details | Repeat: {"description":"LRR 3","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 23 |
| Details | Repeat: {"description":"LRR 4","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 23 |
| Details | Repeat: {"description":"LRR 5","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 26 |
| Details | Repeat: {"description":"LRR 6","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 51 |
| Details | Coiled coil: {"evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"30948527","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6J5T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6J6I","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"30948526","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6J5W","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"O48814","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"O48814","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"O48814","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 9 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
