1WMK
Human death-associated kinase DRP-1, mutant S308D d40
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 |
| E | 0004672 | molecular_function | protein kinase activity |
| E | 0005524 | molecular_function | ATP binding |
| E | 0006468 | biological_process | protein phosphorylation |
| F | 0004672 | molecular_function | protein kinase activity |
| F | 0005524 | molecular_function | ATP binding |
| F | 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 | 28 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGQFAIVKkCrekstgleyaak......FIKK |
| Chain | Residue | Details |
| A | LEU19-LYS46 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IaHfDLKpeNIML |
| Chain | Residue | Details |
| A | ILE135-LEU147 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 |
| Chain | Residue | Details |
| A | ASP139 | |
| E | ASP139 | |
| C | ASP139 | |
| B | ASP139 | |
| F | ASP139 | |
| D | ASP139 | |
| H | ASP139 | |
| G | ASP139 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
| Chain | Residue | Details |
| A | LEU19 | |
| E | LEU19 | |
| C | LEU19 | |
| B | LEU19 | |
| F | LEU19 | |
| D | LEU19 | |
| H | LEU19 | |
| G | LEU19 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:10376525, ECO:0000269|PubMed:10629061 |
| Chain | Residue | Details |
| A | LYS42 | |
| E | LYS42 | |
| C | LYS42 | |
| B | LYS42 | |
| F | LYS42 | |
| D | LYS42 | |
| H | LYS42 | |
| G | LYS42 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER289 | |
| E | SER289 | |
| C | SER289 | |
| B | SER289 | |
| F | SER289 | |
| D | SER289 | |
| H | SER289 | |
| G | SER289 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:11230133 |
| Chain | Residue | Details |
| A | ASP308 | |
| E | ASP308 | |
| C | ASP308 | |
| B | ASP308 | |
| F | ASP308 | |
| D | ASP308 | |
| H | ASP308 | |
| G | ASP308 |
