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 |
| B | 0004672 | molecular_function | protein kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006468 | biological_process | protein phosphorylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 1 |
| Details | binding site for residue IOD A 401 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue IOD A 402 |
| Chain | Residue |
| A | SER24 |
| A | HIS315 |
| A | HOH550 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | binding site for residue IOD A 403 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | binding site for residue IOD A 404 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | binding site for residue IOD A 407 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue CL A 408 |
| Chain | Residue |
| A | LEU54 |
| B | THR49 |
| B | SER51 |
| B | LEU54 |
| A | THR49 |
| A | SER51 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | binding site for residue IOD B 401 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue IOD B 402 |
| Chain | Residue |
| A | LYS20 |
| A | LYS305 |
| B | THR266 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue IOD B 405 |
| Chain | Residue |
| B | PHE23 |
| B | SER24 |
| B | HIS315 |
| site_id | AD1 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 406 |
| Chain | Residue |
| B | LYS316 |
| B | PHE317 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 528 |
| Details | Domain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | Region: {"description":"Calmodulin-binding"} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00100","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"18423203","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"O70589","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"B2RUJ5","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q02410","evidenceCode":"ECO:0000250"}]} |
