3UIM
Structural basis for the impact of phosphorylation on plant receptor-like kinase BAK1 activation
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE ANP A 1000 |
| Chain | Residue |
| A | HOH171 |
| A | TYR365 |
| A | MET366 |
| A | LYS418 |
| A | LEU423 |
| A | ASP434 |
| A | HOH174 |
| A | HOH175 |
| A | LEU295 |
| A | ARG297 |
| A | GLY298 |
| A | VAL303 |
| A | ALA315 |
| A | PRO364 |
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 | 1 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 |
| Chain | Residue | Details |
| A | ASP416 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000305|PubMed:22547027, ECO:0007744|PDB:3UIM |
| Chain | Residue | Details |
| A | LEU295 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
| Chain | Residue | Details |
| A | LYS317 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:22547027, ECO:0007744|PDB:3UIM |
| Chain | Residue | Details |
| A | PRO364 | |
| A | TYR365 | |
| A | MET366 | |
| A | LYS418 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:18694562 |
| Chain | Residue | Details |
| A | SER286 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:15894717, ECO:0000269|PubMed:18694562, ECO:0000269|PubMed:19105183, ECO:0000269|PubMed:22547027 |
| Chain | Residue | Details |
| A | SEP290 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0000269|PubMed:18694562, ECO:0000269|PubMed:22547027 |
| Chain | Residue | Details |
| A | TPO312 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 3 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q94AG2 |
| Chain | Residue | Details |
| A | SER370 | |
| A | SER465 | |
| A | SER470 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9LSI9 |
| Chain | Residue | Details |
| A | SER373 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| 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 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| 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 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0000269|PubMed:15894717, ECO:0000269|PubMed:18694562, ECO:0000269|PubMed:19105183, ECO:0000269|PubMed:22547027 |
| Chain | Residue | Details |
| A | TPO455 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q94AG2 |
| Chain | Residue | Details |
| A | TYR463 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q94AG2 |
| Chain | Residue | Details |
| A | THR466 | |
| A | THR546 |
