3TL8
The AvrPtoB-BAK1 complex reveals two structurally similar kinaseinteracting domains in a single type III effector
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006468 | biological_process | protein phosphorylation |
| D | 0004672 | molecular_function | protein kinase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0006468 | biological_process | protein phosphorylation |
| G | 0004672 | molecular_function | protein kinase activity |
| G | 0005524 | molecular_function | ATP binding |
| G | 0006468 | biological_process | protein phosphorylation |
| H | 0004672 | molecular_function | protein kinase activity |
| H | 0005524 | molecular_function | ATP binding |
| H | 0006468 | biological_process | protein phosphorylation |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 23 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGRGGFGKVYkGrladgtl...........VAVK |
| Chain | Residue | Details |
| A | LEU295-LYS317 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDVKaaNILL |
| Chain | Residue | Details |
| A | ILE412-LEU424 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 |
| Chain | Residue | Details |
| A | ASP416 | |
| D | ASP416 | |
| G | ASP416 | |
| H | ASP416 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000305|PubMed:22547027, ECO:0007744|PDB:3UIM |
| Chain | Residue | Details |
| A | LEU295 | |
| D | LEU295 | |
| G | LEU295 | |
| H | LEU295 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
| Chain | Residue | Details |
| A | LYS317 | |
| D | LYS317 | |
| G | LYS317 | |
| H | LYS317 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:22547027, ECO:0007744|PDB:3UIM |
| Chain | Residue | Details |
| A | PRO364 | |
| G | TYR365 | |
| G | MET366 | |
| G | LYS418 | |
| H | PRO364 | |
| H | TYR365 | |
| H | MET366 | |
| H | LYS418 | |
| A | TYR365 | |
| A | MET366 | |
| A | LYS418 | |
| D | PRO364 | |
| D | TYR365 | |
| D | MET366 | |
| D | LYS418 | |
| G | PRO364 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:18694562 |
| Chain | Residue | Details |
| A | SER286 | |
| D | SER286 | |
| G | SER286 | |
| H | SER286 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:15894717, ECO:0000269|PubMed:18694562, ECO:0000269|PubMed:19105183, ECO:0000269|PubMed:22547027 |
| Chain | Residue | Details |
| A | SER290 | |
| D | SER290 | |
| G | SER290 | |
| H | SER290 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphothreonine => ECO:0000269|PubMed:18694562, ECO:0000269|PubMed:22547027 |
| Chain | Residue | Details |
| A | THR312 | |
| D | THR312 | |
| G | THR312 | |
| H | THR312 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 12 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q94AG2 |
| Chain | Residue | Details |
| A | SER370 | |
| H | SER370 | |
| H | SER465 | |
| H | SER470 | |
| A | SER465 | |
| A | SER470 | |
| D | SER370 | |
| D | SER465 | |
| D | SER470 | |
| G | SER370 | |
| G | SER465 | |
| G | SER470 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9LSI9 |
| Chain | Residue | Details |
| A | SER373 | |
| D | SER373 | |
| G | SER373 | |
| H | SER373 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 8 |
| Details | MOD_RES: Phosphothreonine => ECO:0000269|PubMed:15894717, ECO:0000269|PubMed:18694562, ECO:0000269|PubMed:19105183, ECO:0000269|PubMed:22169508, ECO:0000269|PubMed:22547027 |
| Chain | Residue | Details |
| A | TPO446 | |
| A | TPO449 | |
| D | TPO446 | |
| D | TPO449 | |
| G | TPO446 | |
| G | TPO449 | |
| H | TPO446 | |
| H | TPO449 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphothreonine => ECO:0000269|PubMed:18694562, ECO:0000269|PubMed:19105183, ECO:0000269|PubMed:22169508, ECO:0000269|PubMed:22547027 |
| Chain | Residue | Details |
| A | TPO450 | |
| D | TPO450 | |
| G | TPO450 | |
| H | TPO450 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphothreonine => ECO:0000269|PubMed:15894717, ECO:0000269|PubMed:18694562, ECO:0000269|PubMed:19105183, ECO:0000269|PubMed:22547027 |
| Chain | Residue | Details |
| A | THR455 | |
| D | THR455 | |
| G | THR455 | |
| H | THR455 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q94AG2 |
| Chain | Residue | Details |
| A | TYR463 | |
| D | TYR463 | |
| G | TYR463 | |
| H | TYR463 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 8 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q94AG2 |
| Chain | Residue | Details |
| A | THR466 | |
| A | THR546 | |
| D | THR466 | |
| D | THR546 | |
| G | THR466 | |
| G | THR546 | |
| H | THR466 | |
| H | THR546 |
| site_id | SWS_FT_FI15 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphothreonine => ECO:0000269|PubMed:19105183 |
| Chain | Residue | Details |
| A | THR589 | |
| D | THR589 | |
| G | THR589 | |
| H | THR589 |
