3PFQ
Crystal Structure and Allosteric Activation of Protein Kinase C beta II
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0002250 | biological_process | adaptive immune response |
A | 0003682 | molecular_function | chromatin binding |
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 | 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 | 0010827 | biological_process | regulation of glucose transmembrane transport |
A | 0010829 | biological_process | negative regulation of glucose transmembrane transport |
A | 0014059 | biological_process | regulation of dopamine secretion |
A | 0016020 | cellular_component | membrane |
A | 0018894 | biological_process | dibenzo-p-dioxin metabolic process |
A | 0030374 | molecular_function | nuclear receptor coactivator activity |
A | 0030949 | biological_process | positive regulation of vascular endothelial growth factor receptor signaling pathway |
A | 0031526 | cellular_component | brush border membrane |
A | 0032024 | biological_process | positive regulation of insulin secretion |
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 | 0043687 | biological_process | post-translational protein modification |
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 | 0050861 | biological_process | positive regulation of B cell receptor signaling pathway |
A | 0071322 | biological_process | cellular response to carbohydrate stimulus |
A | 0099171 | biological_process | presynaptic modulation of chemical synaptic transmission |
A | 0099523 | cellular_component | presynaptic cytosol |
A | 0106310 | molecular_function | protein serine kinase activity |
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 | 50 |
Details | ZN_FING: Phorbol-ester/DAG-type 1 => ECO:0000255|PROSITE-ProRule:PRU00226 |
Chain | Residue | Details |
A | ASN36-CYS86 |
site_id | SWS_FT_FI2 |
Number of Residues | 50 |
Details | ZN_FING: Phorbol-ester/DAG-type 2 => ECO:0000255|PROSITE-ProRule:PRU00226 |
Chain | Residue | Details |
A | LYS101-CYS151 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 |
Chain | Residue | Details |
A | ASP466 |
site_id | SWS_FT_FI4 |
Number of Residues | 9 |
Details | BINDING: BINDING => ECO:0000269|PubMed:21215369, ECO:0000269|PubMed:9817842 |
Chain | Residue | Details |
A | MET186 | |
A | ASP187 | |
A | ASP193 | |
A | ASP246 | |
A | TRP247 | |
A | ASP248 | |
A | SER251 | |
A | ARG252 | |
A | ASP254 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
Chain | Residue | Details |
A | LEU348 | |
A | LYS371 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: N-acetylalanine => ECO:0000250|UniProtKB:P05771 |
Chain | Residue | Details |
A | ALA2 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903 |
Chain | Residue | Details |
A | SER11 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:8327493 |
Chain | Residue | Details |
A | SER16 |
site_id | SWS_FT_FI9 |
Number of Residues | 4 |
Details | MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:8327493 |
Chain | Residue | Details |
A | THR17 | |
A | THR314 | |
A | THR324 | |
A | ARG635 |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P05771 |
Chain | Residue | Details |
A | SER206 |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000250 |
Chain | Residue | Details |
A | THR250 |
site_id | SWS_FT_FI12 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine; by PDPK1 => ECO:0000305|PubMed:21215369, ECO:0000305|PubMed:7961692, ECO:0000305|PubMed:8749392 |
Chain | Residue | Details |
A | TPO500 |
site_id | SWS_FT_FI13 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P05771 |
Chain | Residue | Details |
A | THR504 |
site_id | SWS_FT_FI14 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:21215369, ECO:0000269|PubMed:8327493, ECO:0000269|PubMed:8749392, ECO:0007744|PubMed:22673903 |
Chain | Residue | Details |
A | PRO642 |
site_id | SWS_FT_FI15 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:21215369, ECO:0000269|PubMed:8749392 |
Chain | Residue | Details |
A | PHE661 |
site_id | SWS_FT_FI16 |
Number of Residues | 1 |
Details | MOD_RES: Phosphotyrosine; by SYK => ECO:0000250|UniProtKB:P68404 |
Chain | Residue | Details |
A | VAL662 |