3C4X
Crystal Structure of G protein coupled receptor kinase 1 bound to ATP and magnesium chloride at 2.9A
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001750 | cellular_component | photoreceptor outer segment |
| 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 | 0006468 | biological_process | protein phosphorylation |
| A | 0007165 | biological_process | signal transduction |
| A | 0007601 | biological_process | visual perception |
| A | 0009966 | biological_process | regulation of signal transduction |
| A | 0016020 | cellular_component | membrane |
| A | 0022400 | biological_process | regulation of opsin-mediated signaling pathway |
| A | 0042995 | cellular_component | cell projection |
| A | 0046777 | biological_process | protein autophosphorylation |
| A | 0050254 | molecular_function | rhodopsin kinase activity |
| A | 0097381 | cellular_component | photoreceptor disc membrane |
| B | 0001750 | cellular_component | photoreceptor outer segment |
| 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 | 0006468 | biological_process | protein phosphorylation |
| B | 0007165 | biological_process | signal transduction |
| B | 0007601 | biological_process | visual perception |
| B | 0009966 | biological_process | regulation of signal transduction |
| B | 0016020 | cellular_component | membrane |
| B | 0022400 | biological_process | regulation of opsin-mediated signaling pathway |
| B | 0042995 | cellular_component | cell projection |
| B | 0046777 | biological_process | protein autophosphorylation |
| B | 0050254 | molecular_function | rhodopsin kinase activity |
| B | 0097381 | cellular_component | photoreceptor disc membrane |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MG A 564 |
| Chain | Residue |
| A | ASP332 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 565 |
| Chain | Residue |
| A | LEU166 |
| B | GLN173 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 566 |
| Chain | Residue |
| A | GLN287 |
| A | ARG290 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG B 563 |
| Chain | Residue |
| B | ASN319 |
| B | ASP332 |
| site_id | AC5 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE ATP A 562 |
| Chain | Residue |
| A | ARG195 |
| A | GLY196 |
| A | GLY197 |
| A | LYS216 |
| A | THR265 |
| A | MET267 |
| A | LEU321 |
| A | ASP332 |
| A | LYS497 |
| A | ALA498 |
| A | GLU501 |
| A | LEU193 |
| A | GLY194 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ATP B 562 |
| Chain | Residue |
| B | LEU193 |
| B | GLY194 |
| B | GLY196 |
| B | GLY197 |
| B | ALA214 |
| B | LYS216 |
| B | THR265 |
| B | MET267 |
| B | LEU321 |
| B | ASP332 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 24 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGRGGFGEVFaCqmkatgkl..........YACK |
| Chain | Residue | Details |
| A | LEU193-LYS216 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiYrDLKpeNVLL |
| Chain | Residue | Details |
| A | ILE310-LEU322 |
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 | ASP314 | |
| B | ASP314 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:18339619 |
| Chain | Residue | Details |
| A | LEU193 | |
| B | LEU193 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
| Chain | Residue | Details |
| A | LYS216 | |
| B | LYS216 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18339619 |
| Chain | Residue | Details |
| A | THR265 | |
| A | ASP332 | |
| B | THR265 | |
| B | ASP332 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:18339619 |
| Chain | Residue | Details |
| A | SER5 | |
| B | SER5 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine => ECO:0000269|PubMed:18339619 |
| Chain | Residue | Details |
| A | THR8 | |
| B | THR8 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine; by PKA and autocatalysis => ECO:0000305|PubMed:1527025, ECO:0000305|PubMed:18339619 |
| Chain | Residue | Details |
| A | SER21 | |
| B | SER21 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:1527025, ECO:0000269|PubMed:18339619 |
| Chain | Residue | Details |
| A | SER488 | |
| B | SER488 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:1527025, ECO:0000269|PubMed:18339619 |
| Chain | Residue | Details |
| A | THR489 | |
| B | THR489 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP314 | |
| A | GLU318 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASP314 | |
| B | GLU318 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | LYS316 | |
| A | ASP314 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | LYS316 | |
| B | ASP314 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | LYS316 | |
| A | THR352 | |
| A | ASP314 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | LYS316 | |
| B | THR352 | |
| B | ASP314 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | LYS316 | |
| A | ASN319 | |
| A | ASP314 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | LYS316 | |
| B | ASN319 | |
| B | ASP314 |
