6LNM
Crystal structure of CASK-CaMK in complex with Mint1-CID
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 |
| C | 0004672 | molecular_function | protein kinase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006468 | biological_process | protein phosphorylation |
| E | 0004672 | molecular_function | protein kinase activity |
| E | 0005524 | molecular_function | ATP binding |
| E | 0006468 | biological_process | protein phosphorylation |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:21183079 |
| Chain | Residue | Details |
| B | SER372 | |
| D | SER372 | |
| F | SER372 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:21183079 |
| Chain | Residue | Details |
| B | THR375 | |
| D | THR375 | |
| F | THR375 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
| Chain | Residue | Details |
| A | LYS41 | |
| C | LYS41 | |
| E | LYS41 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O14936 |
| Chain | Residue | Details |
| A | SER51 | |
| A | SER313 | |
| C | SER51 | |
| C | SER313 | |
| E | SER51 | |
| E | SER313 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | MOD_RES: Phosphoserine; by autocatalysis => ECO:0000250|UniProtKB:O14936 |
| Chain | Residue | Details |
| A | SER151 | |
| A | SER155 | |
| C | SER151 | |
| C | SER155 | |
| E | SER151 | |
| E | SER155 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 3 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:O70589 |
| Chain | Residue | Details |
| A | THR182 | |
| C | THR182 | |
| E | THR182 |
