2YAA
Crystal structure of the autoinhibited form of mouse DAPK2 in complex with ATP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0004674 | molecular_function | protein serine/threonine kinase activity |
| A | 0005516 | molecular_function | calmodulin binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006468 | biological_process | protein phosphorylation |
| A | 0006915 | biological_process | apoptotic process |
| A | 0031410 | cellular_component | cytoplasmic vesicle |
| A | 0034423 | cellular_component | autophagosome lumen |
| A | 0035556 | biological_process | intracellular signal transduction |
| A | 0043065 | biological_process | positive regulation of apoptotic process |
| A | 0106310 | molecular_function | protein serine kinase activity |
| A | 1990266 | biological_process | neutrophil migration |
| A | 2001242 | biological_process | regulation of intrinsic apoptotic signaling pathway |
| B | 0004672 | molecular_function | protein kinase activity |
| B | 0004674 | molecular_function | protein serine/threonine kinase activity |
| B | 0005516 | molecular_function | calmodulin binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006468 | biological_process | protein phosphorylation |
| B | 0006915 | biological_process | apoptotic process |
| B | 0031410 | cellular_component | cytoplasmic vesicle |
| B | 0034423 | cellular_component | autophagosome lumen |
| B | 0035556 | biological_process | intracellular signal transduction |
| B | 0043065 | biological_process | positive regulation of apoptotic process |
| B | 0106310 | molecular_function | protein serine kinase activity |
| B | 1990266 | biological_process | neutrophil migration |
| B | 2001242 | biological_process | regulation of intrinsic apoptotic signaling pathway |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE ATP A 1302 |
| Chain | Residue |
| A | LEU19 |
| A | ASP139 |
| A | ILE160 |
| A | ASP161 |
| A | HOH2075 |
| A | HOH2082 |
| A | HOH2182 |
| A | GLY22 |
| A | GLN23 |
| A | ALA25 |
| A | VAL27 |
| A | ALA40 |
| A | LYS42 |
| A | GLU94 |
| A | VAL96 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1303 |
| Chain | Residue |
| A | SER49 |
| A | ARG50 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 1304 |
| Chain | Residue |
| A | ASN190 |
| A | HOH2103 |
| A | HOH2106 |
| A | HOH2109 |
| B | ASN190 |
| B | HOH2107 |
| site_id | AC4 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE ATP B 1302 |
| Chain | Residue |
| B | LEU19 |
| B | GLY20 |
| B | SER21 |
| B | GLY22 |
| B | PHE24 |
| B | VAL27 |
| B | ALA40 |
| B | LYS42 |
| B | GLU94 |
| B | VAL96 |
| B | GLU100 |
| B | ASN144 |
| B | ASP161 |
| B | HOH2079 |
| B | HOH2166 |
| B | HOH2167 |
| B | HOH2169 |
| B | HOH2170 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1303 |
| Chain | Residue |
| A | GLN299 |
| B | ARG50 |
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 | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 |
| Chain | Residue | Details |
| A | ASP139 | |
| B | ASP139 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:21497605 |
| Chain | Residue | Details |
| A | LEU19 | |
| A | LYS42 | |
| B | LEU19 | |
| B | LYS42 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079 |
| Chain | Residue | Details |
| A | SER289 | |
| A | SER339 | |
| B | SER289 | |
| B | SER339 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine; by autocatalysis => ECO:0000250|UniProtKB:Q9UIK4 |
| Chain | Residue | Details |
| A | SER308 | |
| B | SER308 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q9UIK4 |
| Chain | Residue | Details |
| A | THR359 | |
| B | THR359 |
