2ACX
Crystal Structure of G protein coupled receptor kinase 6 bound to AMPPNP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0004674 | molecular_function | protein serine/threonine kinase activity |
| A | 0004703 | molecular_function | G protein-coupled receptor kinase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006468 | biological_process | protein phosphorylation |
| A | 0007165 | biological_process | signal transduction |
| A | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
| A | 0008277 | biological_process | regulation of G protein-coupled receptor signaling pathway |
| A | 0009966 | biological_process | regulation of signal transduction |
| A | 0016020 | cellular_component | membrane |
| A | 0016055 | biological_process | Wnt signaling pathway |
| A | 0016310 | biological_process | phosphorylation |
| A | 0047696 | molecular_function | beta-adrenergic receptor kinase activity |
| B | 0004672 | molecular_function | protein kinase activity |
| B | 0004674 | molecular_function | protein serine/threonine kinase activity |
| B | 0004703 | molecular_function | G protein-coupled receptor kinase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006468 | biological_process | protein phosphorylation |
| B | 0007165 | biological_process | signal transduction |
| B | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
| B | 0008277 | biological_process | regulation of G protein-coupled receptor signaling pathway |
| B | 0009966 | biological_process | regulation of signal transduction |
| B | 0016020 | cellular_component | membrane |
| B | 0016055 | biological_process | Wnt signaling pathway |
| B | 0016310 | biological_process | phosphorylation |
| B | 0047696 | molecular_function | beta-adrenergic receptor kinase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MG A 578 |
| Chain | Residue |
| A | ANP577 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MG B 578 |
| Chain | Residue |
| B | ANP577 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 A 579 |
| Chain | Residue |
| A | ALA15 |
| A | ARG16 |
| A | SER27 |
| A | ARG187 |
| A | ARG206 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 B 579 |
| Chain | Residue |
| B | SER27 |
| B | ARG187 |
| B | ARG206 |
| B | ALA15 |
| B | ARG16 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE ANP A 577 |
| Chain | Residue |
| A | ARG123 |
| A | LYS194 |
| A | GLY195 |
| A | GLY196 |
| A | VAL200 |
| A | ALA213 |
| A | LYS215 |
| A | THR264 |
| A | MET266 |
| A | LEU318 |
| A | ASP329 |
| A | MG578 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE ANP B 577 |
| Chain | Residue |
| B | ARG123 |
| B | LYS194 |
| B | GLY195 |
| B | GLY196 |
| B | VAL200 |
| B | ALA213 |
| B | LYS215 |
| B | THR264 |
| B | MET266 |
| B | ASP329 |
| B | MG578 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 33 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGGFGEVCaCqvratgkmyackklekk.RIKK |
| Chain | Residue | Details |
| A | LEU192-LYS224 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvYrDLKpeNILL |
| Chain | Residue | Details |
| A | ILE307-LEU319 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 |
| Chain | Residue | Details |
| A | ASP311 | |
| B | ASP311 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | LEU192 | |
| A | LYS215 | |
| A | THR264 | |
| A | GLU315 | |
| B | LEU192 | |
| B | LYS215 | |
| B | THR264 | |
| B | GLU315 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332 |
| Chain | Residue | Details |
| A | SER484 | |
| B | SER484 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332 |
| Chain | Residue | Details |
| A | THR485 | |
| B | THR485 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O70293 |
| Chain | Residue | Details |
| A | SER566 | |
| A | SER568 | |
| B | SER566 | |
| B | SER568 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | LIPID: S-palmitoyl cysteine => ECO:0000305|PubMed:7961702 |
| Chain | Residue | Details |
| A | SER561 | |
| A | SER562 | |
| A | SER565 | |
| B | SER561 | |
| B | SER562 | |
| B | SER565 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP311 | |
| A | GLU315 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASP311 | |
| B | GLU315 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP311 | |
| A | LYS313 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASP311 | |
| B | LYS313 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | THR348 | |
| A | ASP311 | |
| A | LYS313 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | THR348 | |
| B | ASP311 | |
| B | LYS313 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASN316 | |
| A | ASP311 | |
| A | LYS313 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASN316 | |
| B | ASP311 | |
| B | LYS313 |
