7MX3
Crystal structure of human RIPK3 complexed with GSK'843
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 |
| B | 0004672 | molecular_function | protein kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006468 | biological_process | protein phosphorylation |
| C | 0004672 | molecular_function | protein kinase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006468 | biological_process | protein phosphorylation |
| D | 0004672 | molecular_function | protein kinase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0006468 | biological_process | protein phosphorylation |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 24 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGKGGFGTVFrAqhrkwgyd..........VAVK |
| Chain | Residue | Details |
| A | VAL27-LYS50 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LlHrDLKpsNVLL |
| Chain | Residue | Details |
| A | LEU138-LEU150 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:22265413 |
| Chain | Residue | Details |
| A | ASP142 | |
| B | ASP142 | |
| C | ASP142 | |
| D | ASP142 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
| Chain | Residue | Details |
| A | VAL27 | |
| B | VAL27 | |
| C | VAL27 | |
| D | VAL27 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:10339433, ECO:0000305|PubMed:10358032, ECO:0000305|PubMed:22265414 |
| Chain | Residue | Details |
| A | LYS50 | |
| B | LYS50 | |
| C | LYS50 | |
| D | LYS50 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9QZL0 |
| Chain | Residue | Details |
| A | SER2 | |
| D | SER2 | |
| D | SER164 | |
| D | SER299 | |
| A | SER164 | |
| A | SER299 | |
| B | SER2 | |
| B | SER164 | |
| B | SER299 | |
| C | SER2 | |
| C | SER164 | |
| C | SER299 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphothreonine => ECO:0000269|PubMed:29883609 |
| Chain | Residue | Details |
| A | THR182 | |
| B | THR182 | |
| C | THR182 | |
| D | THR182 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:11734559, ECO:0000269|PubMed:19524512 |
| Chain | Residue | Details |
| A | SER199 | |
| B | SER199 | |
| C | SER199 | |
| D | SER199 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:22265413, ECO:0000269|PubMed:29883609 |
| Chain | Residue | Details |
| A | SER227 | |
| B | SER227 | |
| C | SER227 | |
| D | SER227 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q9QZL0 |
| Chain | Residue | Details |
| A | THR252 | |
| B | THR252 | |
| C | THR252 | |
| D | THR252 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 8 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:33369872 |
| Chain | Residue | Details |
| A | LYS42 | |
| B | LYS42 | |
| C | LYS42 | |
| D | LYS42 |
