2UW3
Structure of PKA-PKB chimera complexed with 5-methyl-4-phenyl-1H- pyrazole
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000287 | molecular_function | magnesium ion binding |
| 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 | 0004691 | molecular_function | cAMP-dependent protein kinase activity |
| A | 0004712 | molecular_function | protein serine/threonine/tyrosine 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 | 0005811 | cellular_component | lipid droplet |
| A | 0005813 | cellular_component | centrosome |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0005930 | cellular_component | axoneme |
| A | 0005952 | cellular_component | cAMP-dependent protein kinase complex |
| A | 0006338 | biological_process | chromatin remodeling |
| A | 0006397 | biological_process | mRNA processing |
| A | 0006468 | biological_process | protein phosphorylation |
| A | 0007189 | biological_process | adenylate cyclase-activating G protein-coupled receptor signaling pathway |
| A | 0007193 | biological_process | adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway |
| A | 0010898 | biological_process | positive regulation of triglyceride catabolic process |
| A | 0016020 | cellular_component | membrane |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016607 | cellular_component | nuclear speck |
| A | 0016740 | molecular_function | transferase activity |
| A | 0019901 | molecular_function | protein kinase binding |
| A | 0019904 | molecular_function | protein domain specific binding |
| A | 0030007 | biological_process | intracellular potassium ion homeostasis |
| A | 0030145 | molecular_function | manganese ion 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 | 0044853 | cellular_component | plasma membrane raft |
| A | 0045542 | biological_process | positive regulation of cholesterol biosynthetic process |
| A | 0045667 | biological_process | regulation of osteoblast differentiation |
| A | 0045722 | biological_process | positive regulation of gluconeogenesis |
| A | 0045820 | biological_process | negative regulation of glycolytic process |
| A | 0048240 | biological_process | sperm capacitation |
| A | 0048471 | cellular_component | perinuclear region of cytoplasm |
| A | 0050766 | biological_process | positive regulation of phagocytosis |
| A | 0051726 | biological_process | regulation of cell cycle |
| A | 0061136 | biological_process | regulation of proteasomal protein catabolic process |
| A | 0070507 | biological_process | regulation of microtubule cytoskeleton organization |
| A | 0071333 | biological_process | cellular response to glucose stimulus |
| A | 0071377 | biological_process | cellular response to glucagon stimulus |
| A | 0097546 | cellular_component | ciliary base |
| A | 0098794 | cellular_component | postsynapse |
| A | 0098978 | cellular_component | glutamatergic synapse |
| A | 0099170 | biological_process | postsynaptic modulation of chemical synaptic transmission |
| A | 0106310 | molecular_function | protein serine kinase activity |
| A | 0120186 | biological_process | negative regulation of protein localization to chromatin |
| A | 0140198 | molecular_function | histone H1-4S35 kinase activity |
| A | 1904262 | biological_process | negative regulation of TORC1 signaling |
| A | 1904539 | biological_process | negative regulation of glycolytic process through fructose-6-phosphate |
| A | 2000810 | biological_process | regulation of bicellular tight junction assembly |
| 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 | 8 |
| Details | BINDING SITE FOR RESIDUE GVG A1351 |
| Chain | Residue |
| A | LEU49 |
| A | VAL57 |
| A | ALA70 |
| A | GLU121 |
| A | TYR122 |
| A | ALA123 |
| A | MET173 |
| A | THR183 |
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 | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"6286662","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 9 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 9 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P17612","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P05132","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine; by PDPK1","evidences":[{"source":"PubMed","id":"6262777","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P05132","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"6262777","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 3 |
| Details | Site: {"description":"Important for inhibition","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
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 | GLU170 | activator, proton acceptor, proton donor |
| A | LEU172 | electrostatic stabiliser, polar interaction |
| A | ASP175 | metal ligand |
| A | ALA188 | metal ligand |
| A | ILE209 | electrostatic stabiliser, polar interaction |
