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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | binding site for residue XIN A 401 |
| Chain | Residue |
| A | MET26 |
| A | VAL104 |
| A | MET126 |
| A | ASP127 |
| A | PHE128 |
| A | CYS129 |
| A | ARG130 |
| A | GLY132 |
| A | GLN133 |
| A | ASN136 |
| A | LEU183 |
| A | SER32 |
| A | ASP194 |
| A | HOH645 |
| A | HOH668 |
| A | ILE35 |
| A | ASP49 |
| A | GLU50 |
| A | LEU52 |
| A | ALA53 |
| A | ALA72 |
| A | MET94 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue PEG A 402 |
| Chain | Residue |
| A | LYS242 |
| A | ASP299 |
| A | LYS300 |
| A | ARG301 |
| A | GLN306 |
| A | SER327 |
| A | HOH532 |
| A | HOH553 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | binding site for residue GOL A 403 |
| Chain | Residue |
| A | LEU142 |
| A | GLN143 |
| A | GLY145 |
| A | CYS256 |
| A | PHE258 |
| A | PRO322 |
| A | GOL407 |
| A | HOH529 |
| A | HOH571 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 404 |
| Chain | Residue |
| A | LEU97 |
| A | HIS100 |
| A | ARG164 |
| A | ASP278 |
| A | GLN284 |
| A | HIS287 |
| A | HOH513 |
| A | HOH517 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | binding site for residue GOL A 405 |
| Chain | Residue |
| A | PHE202 |
| A | THR240 |
| A | THR241 |
| A | ASP303 |
| A | GLN325 |
| A | GOL408 |
| A | HOH531 |
| A | HOH532 |
| A | HOH568 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 406 |
| Chain | Residue |
| A | VAL210 |
| A | ASN211 |
| A | GLU264 |
| A | SER265 |
| A | GLN266 |
| A | HOH551 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 407 |
| Chain | Residue |
| A | TYR257 |
| A | SER280 |
| A | ARG281 |
| A | GOL403 |
| A | HOH540 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 408 |
| Chain | Residue |
| A | LYS237 |
| A | ILE238 |
| A | THR240 |
| A | LYS242 |
| A | ASP299 |
| A | GOL405 |
| A | HOH524 |
| A | HOH577 |
| site_id | AC9 |
| Number of Residues | 11 |
| Details | binding site for residue GOL A 409 |
| Chain | Residue |
| A | SER98 |
| A | HIS100 |
| A | LYS101 |
| A | ILE103 |
| A | VAL104 |
| A | GLY105 |
| A | ASP127 |
| A | HIS189 |
| A | HOH526 |
| A | HOH587 |
| A | HOH685 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 410 |
| Chain | Residue |
| A | LYS218 |
| A | ARG226 |
| A | HOH618 |
| A | HOH652 |
Functional Information from PROSITE/UniProt
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDLKveNILL |
| Chain | Residue | Details |
| A | ILE172-LEU184 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 9 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"}]} |
