8BFM
Crystal structure of human calmodulin-dependent protein kinase 1D (CAMK1D) in complex with FZ331
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 | 0004683 | molecular_function | calmodulin-dependent protein kinase activity |
| A | 0005515 | molecular_function | protein binding |
| 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 | 0006954 | biological_process | inflammatory response |
| A | 0007399 | biological_process | nervous system development |
| A | 0010976 | biological_process | positive regulation of neuron projection development |
| A | 0032793 | biological_process | positive regulation of CREB transcription factor activity |
| A | 0043065 | biological_process | positive regulation of apoptotic process |
| A | 0043066 | biological_process | negative regulation of apoptotic process |
| A | 0050766 | biological_process | positive regulation of phagocytosis |
| A | 0050773 | biological_process | regulation of dendrite development |
| A | 0060267 | biological_process | positive regulation of respiratory burst |
| A | 0071622 | biological_process | regulation of granulocyte chemotaxis |
| A | 0090023 | biological_process | positive regulation of neutrophil chemotaxis |
| A | 0106310 | molecular_function | protein serine kinase activity |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 29 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGTGAFSEVVlAeekatgklfavkc.....IPKK |
| Chain | Residue | Details |
| A | LEU29-LYS57 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvHrDLKpeNLLY |
| Chain | Residue | Details |
| A | ILE140-TYR152 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 |
| Chain | Residue | Details |
| A | ASP144 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
| Chain | Residue | Details |
| A | LEU29 | |
| A | LYS52 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648 |
| Chain | Residue | Details |
| A | SER122 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine; by CaMKK1 and CaMKK2 => ECO:0000269|PubMed:12935886, ECO:0007744|PubMed:18669648 |
| Chain | Residue | Details |
| A | THR180 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25218447 |
| Chain | Residue | Details |
| A | LYS113 |
