2VO6
Structure of PKA-PKB chimera complexed with 4-(4-Chlorobenzyl)-1-(7H- pyrrolo(2,3-d)pyrimidin-4-yl)piperidin-4-ylamine
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 | 4 |
| Details | BINDING SITE FOR RESIDUE CL A1351 |
| Chain | Residue |
| A | LYS72 |
| A | ASP184 |
| A | M051352 |
| A | HOH2143 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE M05 A1352 |
| Chain | Residue |
| A | ALA70 |
| A | THR104 |
| A | GLU121 |
| A | ALA123 |
| A | GLU127 |
| A | GLU170 |
| A | ASN171 |
| A | MET173 |
| A | THR183 |
| A | ASP184 |
| A | CL1351 |
| A | GLY50 |
| A | THR51 |
| A | GLY52 |
| A | GLY55 |
| A | ARG56 |
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. LiYrDLKpeNLMI |
| 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 | ARG15 | |
| I | ARG18 | |
| I | ARG19 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | LEU49 | |
| A | LYS72 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
| Chain | Residue | Details |
| A | GLU121 | |
| A | LYS168 |
| 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 | ASN2 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine; by autocatalysis => ECO:0000250|UniProtKB:P05132 |
| Chain | Residue | Details |
| A | SER10 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P17612 |
| Chain | Residue | Details |
| A | THR48 | |
| A | THR195 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P05132 |
| Chain | Residue | Details |
| A | SEP139 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine; by PDPK1 => ECO:0000269|PubMed:6262777 |
| Chain | Residue | Details |
| A | TPO197 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P05132 |
| Chain | Residue | Details |
| A | TYR330 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:6262777 |
| Chain | Residue | Details |
| A | SEP338 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | LIPID: N-myristoyl glycine => ECO:0000269|PubMed:6262777 |
| Chain | Residue | Details |
| A | GLY1 |
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 | ASP166 | activator, proton acceptor, proton donor |
| A | LYS168 | electrostatic stabiliser, polar interaction |
| A | ASN171 | metal ligand |
| A | ASP184 | metal ligand |
| A | THR201 | electrostatic stabiliser, polar interaction |
