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 | 8 |
Details | BINDING SITE FOR RESIDUE SO4 B 342 |
Chain | Residue |
A | HIS86 |
A | SER89 |
A | ARG90 |
A | ARG93 |
B | HIS86 |
B | SER89 |
B | ARG90 |
B | ARG93 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 342 |
Chain | Residue |
A | PHE236 |
A | LYS239 |
A | ARG240 |
A | HOH363 |
A | HIS162 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 24 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGAYAKVQgAvslqngke..........YAVK |
Chain | Residue | Details |
A | LEU55-LYS78 | |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IaHrDLKpeNILC |
Chain | Residue | Details |
A | ILE166-CYS178 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
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"}]} |
site_id | SWS_FT_FI2 |
Number of Residues | 16 |
Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11463832","evidenceCode":"ECO:0000269"}]} |
site_id | SWS_FT_FI4 |
Number of Residues | 5 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | ASP170 | |
A | GLU174 | |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
B | ASP170 | |
B | GLU174 | |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | LYS172 | |
A | ASP170 | |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
B | LYS172 | |
B | ASP170 | |
site_id | CSA5 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | ASN175 | |
A | LYS172 | |
A | ASP170 | |
site_id | CSA6 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
B | ASN175 | |
B | LYS172 | |
B | ASP170 | |