2C1A
Structure of cAMP-dependent protein kinase complexed with Isoquinoline-5-sulfonic acid (2-(2-(4-chlorobenzyloxy)ethylamino) ethyl)amide
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0001669 | cellular_component | acrosomal vesicle |
A | 0001707 | biological_process | mesoderm formation |
A | 0004672 | molecular_function | protein kinase activity |
A | 0004674 | molecular_function | protein serine/threonine kinase activity |
A | 0004679 | molecular_function | AMP-activated protein kinase activity |
A | 0004691 | molecular_function | cAMP-dependent protein kinase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005524 | molecular_function | ATP binding |
A | 0005634 | cellular_component | nucleus |
A | 0005737 | cellular_component | cytoplasm |
A | 0005739 | cellular_component | mitochondrion |
A | 0005829 | cellular_component | cytosol |
A | 0005886 | cellular_component | plasma membrane |
A | 0005952 | cellular_component | cAMP-dependent protein kinase complex |
A | 0006468 | biological_process | protein phosphorylation |
A | 0010737 | biological_process | protein kinase A signaling |
A | 0016310 | biological_process | phosphorylation |
A | 0018105 | biological_process | peptidyl-serine phosphorylation |
A | 0019904 | molecular_function | protein domain specific binding |
A | 0031594 | cellular_component | neuromuscular junction |
A | 0034237 | molecular_function | protein kinase A regulatory subunit binding |
A | 0034605 | biological_process | cellular response to heat |
A | 0036126 | cellular_component | sperm flagellum |
A | 0048471 | cellular_component | perinuclear region of cytoplasm |
A | 0106310 | molecular_function | protein serine kinase activity |
A | 1904262 | biological_process | negative regulation of TORC1 signaling |
I | 0004862 | molecular_function | cAMP-dependent protein kinase inhibitor activity |
I | 0006469 | biological_process | negative regulation of protein kinase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE I5S A1351 |
Chain | Residue |
A | LEU49 |
A | TYR122 |
A | VAL123 |
A | GLU127 |
A | GLU170 |
A | ASN171 |
A | LEU173 |
A | THR183 |
A | ASP184 |
A | PHE327 |
I | HOH2022 |
A | GLY50 |
A | THR51 |
A | GLY52 |
A | GLY55 |
A | ARG56 |
A | VAL57 |
A | ALA70 |
A | GLU121 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 24 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGTGSFGRVMlVkhmetgnh..........YAMK |
Chain | Residue | Details |
A | LEU49-LYS72 |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LiYrDLKpeNLLI |
Chain | Residue | Details |
A | LEU162-ILE174 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | SITE: Important for inhibition => ECO:0000250 |
Chain | Residue | Details |
I | THR16 | |
I | ARG19 | |
I | ASN20 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: |
Chain | Residue | Details |
A | GLY50 | |
A | ILE73 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
Chain | Residue | Details |
A | TYR122 | |
A | PRO169 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: Deamidated asparagine; partial => ECO:0000269|PubMed:10684253, ECO:0000269|PubMed:11152138, ECO:0000269|PubMed:9521123 |
Chain | Residue | Details |
A | ALA3 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by autocatalysis => ECO:0000250|UniProtKB:P05132 |
Chain | Residue | Details |
A | GLU11 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P17612 |
Chain | Residue | Details |
A | LEU49 | |
A | TRP196 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P05132 |
Chain | Residue | Details |
A | GLU140 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine; by PDPK1 => ECO:0000269|PubMed:6262777 |
Chain | Residue | Details |
A | LEU198 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P05132 |
Chain | Residue | Details |
A | GLU331 |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:6262777 |
Chain | Residue | Details |
A | ILE339 |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | LIPID: N-myristoyl glycine => ECO:0000269|PubMed:6262777 |
Chain | Residue | Details |
A | ASN2 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | GLU170 | |
A | ASP166 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | ASP166 | |
A | LYS168 |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | THR201 | |
A | ASP166 | |
A | LYS168 |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | ASP166 | |
A | ASN171 | |
A | LYS168 |
site_id | MCSA1 |
Number of Residues | 5 |
Details | M-CSA 757 |
Chain | Residue | Details |
A | LEU167 | activator, proton acceptor, proton donor |
A | PRO169 | electrostatic stabiliser, polar interaction |
A | LEU172 | metal ligand |
A | PHE185 | metal ligand |
A | PRO202 | electrostatic stabiliser, polar interaction |