3PFQ
Crystal Structure and Allosteric Activation of Protein Kinase C beta II
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0001666 | biological_process | response to hypoxia |
| A | 0002250 | biological_process | adaptive immune response |
| A | 0002376 | biological_process | immune system process |
| A | 0003682 | molecular_function | chromatin binding |
| A | 0003713 | molecular_function | transcription coactivator activity |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0004674 | molecular_function | protein serine/threonine kinase activity |
| A | 0004697 | molecular_function | diacylglycerol-dependent serine/threonine kinase activity |
| A | 0004698 | molecular_function | calcium,diacylglycerol-dependent serine/threonine kinase activity |
| A | 0005080 | molecular_function | protein kinase C binding |
| A | 0005246 | molecular_function | calcium channel regulator activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005813 | cellular_component | centrosome |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006325 | biological_process | chromatin organization |
| A | 0006338 | biological_process | chromatin remodeling |
| A | 0006357 | biological_process | regulation of transcription by RNA polymerase II |
| A | 0006468 | biological_process | protein phosphorylation |
| A | 0006816 | biological_process | calcium ion transport |
| A | 0006874 | biological_process | intracellular calcium ion homeostasis |
| A | 0006915 | biological_process | apoptotic process |
| A | 0007207 | biological_process | phospholipase C-activating G protein-coupled acetylcholine receptor signaling pathway |
| A | 0008091 | cellular_component | spectrin |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0009410 | biological_process | response to xenobiotic stimulus |
| A | 0009749 | biological_process | response to glucose |
| A | 0009966 | biological_process | regulation of signal transduction |
| A | 0010827 | biological_process | regulation of D-glucose transmembrane transport |
| A | 0010829 | biological_process | negative regulation of D-glucose transmembrane transport |
| A | 0014059 | biological_process | regulation of dopamine secretion |
| A | 0016020 | cellular_component | membrane |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0018894 | biological_process | dibenzo-p-dioxin metabolic process |
| A | 0030949 | biological_process | positive regulation of vascular endothelial growth factor receptor signaling pathway |
| A | 0031526 | cellular_component | brush border membrane |
| A | 0033280 | biological_process | response to vitamin D |
| A | 0035403 | molecular_function | histone H3T6 kinase activity |
| A | 0035556 | biological_process | intracellular signal transduction |
| A | 0040008 | biological_process | regulation of growth |
| A | 0042113 | biological_process | B cell activation |
| A | 0042393 | molecular_function | histone binding |
| A | 0042488 | biological_process | positive regulation of odontogenesis of dentin-containing tooth |
| A | 0043123 | biological_process | positive regulation of canonical NF-kappaB signal transduction |
| A | 0044305 | cellular_component | calyx of Held |
| A | 0045471 | biological_process | response to ethanol |
| A | 0045766 | biological_process | positive regulation of angiogenesis |
| A | 0045893 | biological_process | positive regulation of DNA-templated transcription |
| A | 0046627 | biological_process | negative regulation of insulin receptor signaling pathway |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050681 | molecular_function | nuclear androgen receptor binding |
| A | 0050853 | biological_process | B cell receptor signaling pathway |
| A | 0051094 | biological_process | positive regulation of developmental process |
| A | 0051240 | biological_process | positive regulation of multicellular organismal process |
| A | 0070528 | biological_process | protein kinase C signaling |
| A | 0071322 | biological_process | cellular response to carbohydrate stimulus |
| A | 0099523 | cellular_component | presynaptic cytosol |
| A | 0106310 | molecular_function | protein serine kinase activity |
| A | 0160020 | biological_process | positive regulation of ferroptosis |
| A | 1903530 | biological_process | regulation of secretion by cell |
| A | 1990776 | biological_process | response to angiotensin |
| A | 2000300 | biological_process | regulation of synaptic vesicle exocytosis |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 674 |
| Chain | Residue |
| A | ASP187 |
| A | ASP193 |
| A | ASP246 |
| A | TRP247 |
| A | ASP248 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 675 |
| Chain | Residue |
| A | ASP254 |
| A | MET186 |
| A | ASP187 |
| A | ASP246 |
| A | ASP248 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA A 676 |
| Chain | Residue |
| A | ASP248 |
| A | SER251 |
| A | ARG252 |
| A | ASP254 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN A 750 |
| Chain | Residue |
| A | HIS102 |
| A | THR134 |
| A | CYS135 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 751 |
| Chain | Residue |
| A | CYS115 |
| A | CYS118 |
| A | HIS140 |
| A | CYS143 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ANP A 800 |
| Chain | Residue |
| A | ALA369 |
| A | LYS371 |
| A | MET420 |
| A | GLU421 |
| A | TYR422 |
| A | VAL423 |
| A | ASP484 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 24 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGSFGKVMlSerkgtdel..........YAVK |
| Chain | Residue | Details |
| A | LEU348-LYS371 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiYrDLKldNVML |
| Chain | Residue | Details |
| A | ILE462-LEU474 |
| site_id | PS00479 |
| Number of Residues | 50 |
| Details | ZF_DAG_PE_1 Zinc finger phorbol-ester/DAG-type signature. HkFtarffkqptf.CshCtdfIwgfgkqgfq.CqvCsfvvHkrChefvtfs..C |
| Chain | Residue | Details |
| A | HIS37-CYS86 | |
| A | HIS102-CYS151 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 117 |
| Details | Domain: {"description":"C2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00041","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 50 |
| Details | Zinc finger: {"description":"Phorbol-ester/DAG-type 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00226","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| 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"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 9 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21215369","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9817842","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 9 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P05771","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine; by PDPK1","evidences":[{"source":"PubMed","id":"21215369","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"7961692","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"8749392","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P05771","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"8327493","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"21215369","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8327493","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8749392","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22673903","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"22673903","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"22673903","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
