9LFV
Crystal structure of mouse RIP3 kinase domain complexed with LK01004
This is a non-PDB format compatible entry.
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 24 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGKGGFGVVFrAhhrtwnhd..........VAVK |
| Chain | Residue | Details |
| A | VAL28-LYS51 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LlHrDLKpsNILL |
| Chain | Residue | Details |
| A | LEU139-LEU151 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:10490590, ECO:0000305|PubMed:24095729 |
| Chain | Residue | Details |
| A | ASP143 | |
| B | ASP143 | |
| C | ASP143 | |
| D | ASP143 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:24095729, ECO:0007744|PDB:4M69 |
| Chain | Residue | Details |
| A | VAL28 | |
| B | VAL28 | |
| C | VAL28 | |
| D | VAL28 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:24095729, ECO:0007744|PDB:4M69 |
| Chain | Residue | Details |
| A | LYS51 | |
| B | LYS51 | |
| C | LYS51 | |
| D | LYS51 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:23612963 |
| Chain | Residue | Details |
| A | SER2 | |
| D | SER2 | |
| D | SER165 | |
| D | SER300 | |
| A | SER165 | |
| A | SER300 | |
| B | SER2 | |
| B | SER165 | |
| B | SER300 | |
| C | SER2 | |
| C | SER165 | |
| C | SER300 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q9Y572 |
| Chain | Residue | Details |
| A | THR183 | |
| B | THR167 | |
| C | THR166 | |
| D | THR183 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine; by autocatalysis => ECO:0000250|UniProtKB:Q9Y572 |
| Chain | Residue | Details |
| A | SER200 | |
| B | SER200 | |
| C | SER200 | |
| D | SER200 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:23612963, ECO:0000269|PubMed:27819682 |
| Chain | Residue | Details |
| A | THR227 | |
| B | THR227 | |
| C | THR227 | |
| D | THR227 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:23612963, ECO:0000269|PubMed:27819682 |
| Chain | Residue | Details |
| A | SER228 | |
| B | SER228 | |
| C | SER228 | |
| D | SER228 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphothreonine => ECO:0000269|PubMed:23612963 |
| Chain | Residue | Details |
| A | THR253 | |
| B | THR253 | |
| C | THR253 | |
| D | THR253 |
