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 | 10 |
Details | BINDING SITE FOR RESIDUE XDR A 309 |
Chain | Residue |
A | LEU17 |
A | VAL155 |
A | GLY18 |
A | VAL25 |
A | ALA38 |
A | GLU93 |
A | VAL95 |
A | GLY97 |
A | ALA142 |
A | ASN143 |
site_id | AC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 A 310 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 311 |
Chain | Residue |
A | ALA256 |
A | LYS257 |
A | ASN258 |
A | ASN261 |
site_id | AC4 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE XDR B 309 |
Chain | Residue |
B | LEU17 |
B | GLY18 |
B | ALA38 |
B | LYS40 |
B | GLU93 |
B | VAL95 |
B | THR99 |
B | ALA142 |
B | ASN143 |
B | LEU145 |
B | VAL155 |
B | ASP156 |
site_id | AC5 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE SO4 B 310 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 B 311 |
Chain | Residue |
B | ALA256 |
B | LYS257 |
B | ASN258 |
B | ASN261 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 24 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGFGGMSEVHlArdlrdhrd..........VAVK |
Chain | Residue | Details |
A | LEU17-LYS40 | |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDVKpaNILI |
Chain | Residue | Details |
A | ILE134-ILE146 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor |
Chain | Residue | Details |
A | ASP138 | |
B | ASP138 | |
Chain | Residue | Details |
A | LEU17 | |
A | LYS40 | |
A | GLU93 | |
A | LYS140 | |
B | LEU17 | |
B | LYS40 | |
B | GLU93 | |
B | LYS140 | |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: |
Chain | Residue | Details |
A | ASN143 | |
A | ASP156 | |
B | ASN143 | |
B | ASP156 | |
Chain | Residue | Details |
A | THR2 | |
B | THR2 | |
Chain | Residue | Details |
A | SER166 | |
B | SER166 | |
Chain | Residue | Details |
A | SER169 | |
A | SER295 | |
B | SER169 | |
B | SER295 | |
Chain | Residue | Details |
A | TPO171 | |
B | TPO171 | |
Chain | Residue | Details |
A | THR173 | |
B | THR173 | |
Chain | Residue | Details |
A | THR294 | |
B | THR294 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | ALA142 | |
A | ASP138 | |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
B | ALA142 | |
B | ASP138 | |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | ASP138 | |
A | LYS140 | |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
B | ASP138 | |
B | LYS140 | |
site_id | CSA5 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | THR179 | |
A | ASP138 | |
A | LYS140 | |
site_id | CSA6 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
B | THR179 | |
B | ASP138 | |
B | LYS140 | |
site_id | CSA7 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | ASP138 | |
A | ASN143 | |
A | LYS140 | |
site_id | CSA8 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
B | ASP138 | |
B | ASN143 | |
B | LYS140 | |