2YAB
Crystal structure of the autoinhibited form of mouse DAPK2 in complex with AMP
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 | 17 |
Details | BINDING SITE FOR RESIDUE AMP A 1302 |
Chain | Residue |
A | LEU19 |
A | ILE160 |
A | ASP161 |
A | HOH2171 |
A | HOH2345 |
A | HOH2346 |
A | HOH2347 |
A | HOH2348 |
A | HOH2349 |
A | GLY20 |
A | SER21 |
A | ALA25 |
A | VAL27 |
A | ALA40 |
A | LYS42 |
A | GLU94 |
A | VAL96 |
site_id | AC2 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE SO4 A 1303 |
Chain | Residue |
A | ARG271 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 1304 |
Chain | Residue |
A | ASN190 |
A | HOH2222 |
A | HOH2225 |
B | ASN190 |
B | HOH2226 |
B | HOH2232 |
site_id | AC4 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE AMP B 1302 |
Chain | Residue |
B | LEU19 |
B | GLY20 |
B | SER21 |
B | VAL27 |
B | ALA40 |
B | LYS42 |
B | ILE77 |
B | GLU94 |
B | VAL96 |
B | GLU100 |
B | ASN144 |
B | ASP161 |
B | HOH2041 |
B | HOH2326 |
B | HOH2327 |
B | HOH2328 |
B | HOH2329 |
B | HOH2330 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 B 1303 |
Chain | Residue |
B | LYS108 |
B | GLU109 |
B | SER110 |
B | HOH2155 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B 1304 |
Chain | Residue |
A | GLN299 |
B | SER49 |
B | ARG50 |
B | HOH2331 |
B | HOH2332 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 B 1305 |
Chain | Residue |
A | LYS222 |
B | ARG47 |
B | HOH2097 |
B | HOH2333 |
B | HOH2334 |
B | HOH2335 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 B 1306 |
Chain | Residue |
A | ARG47 |
A | HOH2072 |
B | LYS222 |
B | HOH2337 |
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 |