2YA9
Crystal structure of the autoinhibited form of mouse DAPK2
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 | 0005794 | cellular_component | Golgi apparatus |
| A | 0006468 | biological_process | protein phosphorylation |
| A | 0034423 | cellular_component | autophagosome lumen |
| A | 0035556 | biological_process | intracellular signal transduction |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0043065 | biological_process | positive regulation of apoptotic process |
| A | 0043276 | biological_process | anoikis |
| A | 0090023 | biological_process | positive regulation of neutrophil chemotaxis |
| A | 0106310 | molecular_function | protein serine kinase activity |
| A | 1990266 | biological_process | neutrophil migration |
| A | 2000424 | biological_process | positive regulation of eosinophil chemotaxis |
| 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 | 0005794 | cellular_component | Golgi apparatus |
| B | 0006468 | biological_process | protein phosphorylation |
| B | 0034423 | cellular_component | autophagosome lumen |
| B | 0035556 | biological_process | intracellular signal transduction |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0043065 | biological_process | positive regulation of apoptotic process |
| B | 0043276 | biological_process | anoikis |
| B | 0090023 | biological_process | positive regulation of neutrophil chemotaxis |
| B | 0106310 | molecular_function | protein serine kinase activity |
| B | 1990266 | biological_process | neutrophil migration |
| B | 2000424 | biological_process | positive regulation of eosinophil chemotaxis |
| B | 2001242 | biological_process | regulation of intrinsic apoptotic signaling pathway |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE D1D A 1302 |
| Chain | Residue |
| A | PHE178 |
| A | GLY179 |
| A | HOH2206 |
| A | HOH2207 |
| B | ILE177 |
| B | D1D1302 |
| B | HOH2206 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 1303 |
| Chain | Residue |
| A | HOH2122 |
| B | ASN190 |
| B | HOH2121 |
| B | HOH2127 |
| A | ASN190 |
| A | HOH2115 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE D1D B 1302 |
| Chain | Residue |
| A | D1D1302 |
| A | HOH2206 |
| B | PHE178 |
| B | GLY179 |
| B | HOH2206 |
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 | 524 |
| Details | Domain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 18 |
| Details | Region: {"description":"Autoinhibitory domain"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21497605","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17242355","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21183079","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
