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3PFQ

Crystal Structure and Allosteric Activation of Protein Kinase C beta II

Functional Information from GO Data
ChainGOidnamespacecontents
A0002250biological_processadaptive immune response
A0003682molecular_functionchromatin binding
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0004697molecular_functiondiacylglycerol-dependent serine/threonine kinase activity
A0005080molecular_functionprotein kinase C binding
A0005246molecular_functioncalcium channel regulator activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005813cellular_componentcentrosome
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006325biological_processchromatin organization
A0006338biological_processchromatin remodeling
A0006357biological_processregulation of transcription by RNA polymerase II
A0006468biological_processprotein phosphorylation
A0006816biological_processcalcium ion transport
A0006874biological_processintracellular calcium ion homeostasis
A0006915biological_processapoptotic process
A0007207biological_processphospholipase C-activating G protein-coupled acetylcholine receptor signaling pathway
A0008091cellular_componentspectrin
A0008270molecular_functionzinc ion binding
A0009410biological_processresponse to xenobiotic stimulus
A0009749biological_processresponse to glucose
A0010827biological_processregulation of glucose transmembrane transport
A0010829biological_processnegative regulation of glucose transmembrane transport
A0014059biological_processregulation of dopamine secretion
A0016020cellular_componentmembrane
A0018894biological_processdibenzo-p-dioxin metabolic process
A0030374molecular_functionnuclear receptor coactivator activity
A0030949biological_processpositive regulation of vascular endothelial growth factor receptor signaling pathway
A0031526cellular_componentbrush border membrane
A0032024biological_processpositive regulation of insulin secretion
A0033280biological_processresponse to vitamin D
A0035403molecular_functionhistone H3T6 kinase activity
A0035556biological_processintracellular signal transduction
A0040008biological_processregulation of growth
A0042113biological_processB cell activation
A0042393molecular_functionhistone binding
A0042488biological_processpositive regulation of odontogenesis of dentin-containing tooth
A0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
A0043687biological_processpost-translational protein modification
A0044305cellular_componentcalyx of Held
A0045471biological_processresponse to ethanol
A0045766biological_processpositive regulation of angiogenesis
A0045893biological_processpositive regulation of DNA-templated transcription
A0046627biological_processnegative regulation of insulin receptor signaling pathway
A0046872molecular_functionmetal ion binding
A0050681molecular_functionnuclear androgen receptor binding
A0050853biological_processB cell receptor signaling pathway
A0050861biological_processpositive regulation of B cell receptor signaling pathway
A0071322biological_processcellular response to carbohydrate stimulus
A0099171biological_processpresynaptic modulation of chemical synaptic transmission
A0099523cellular_componentpresynaptic cytosol
A0106310molecular_functionprotein serine kinase activity
A2000300biological_processregulation of synaptic vesicle exocytosis
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 674
ChainResidue
AASP187
AASP193
AASP246
ATRP247
AASP248

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 675
ChainResidue
AASP254
AMET186
AASP187
AASP246
AASP248

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 676
ChainResidue
AASP248
ASER251
AARG252
AASP254

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN A 750
ChainResidue
AHIS102
ATHR134
ACYS135

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 751
ChainResidue
ACYS115
ACYS118
AHIS140
ACYS143

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ANP A 800
ChainResidue
AALA369
ALYS371
AMET420
AGLU421
ATYR422
AVAL423
AASP484

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGSFGKVMlSerkgtdel..........YAVK
ChainResidueDetails
ALEU348-LYS371

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiYrDLKldNVML
ChainResidueDetails
AILE462-LEU474

site_idPS00479
Number of Residues50
DetailsZF_DAG_PE_1 Zinc finger phorbol-ester/DAG-type signature. HkFtarffkqptf.CshCtdfIwgfgkqgfq.CqvCsfvvHkrChefvtfs..C
ChainResidueDetails
AHIS37-CYS86
AHIS102-CYS151

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues50
DetailsZN_FING: Phorbol-ester/DAG-type 1 => ECO:0000255|PROSITE-ProRule:PRU00226
ChainResidueDetails
AASN36-CYS86

site_idSWS_FT_FI2
Number of Residues50
DetailsZN_FING: Phorbol-ester/DAG-type 2 => ECO:0000255|PROSITE-ProRule:PRU00226
ChainResidueDetails
ALYS101-CYS151

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
AASP466

site_idSWS_FT_FI4
Number of Residues9
DetailsBINDING: BINDING => ECO:0000269|PubMed:21215369, ECO:0000269|PubMed:9817842
ChainResidueDetails
AMET186
AASP187
AASP193
AASP246
ATRP247
AASP248
ASER251
AARG252
AASP254

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU348
ALYS371

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000250|UniProtKB:P05771
ChainResidueDetails
AALA2

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903
ChainResidueDetails
ASER11

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:8327493
ChainResidueDetails
ASER16

site_idSWS_FT_FI9
Number of Residues4
DetailsMOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:8327493
ChainResidueDetails
ATHR17
ATHR314
ATHR324
AARG635

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P05771
ChainResidueDetails
ASER206

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by autocatalysis => ECO:0000250
ChainResidueDetails
ATHR250

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by PDPK1 => ECO:0000305|PubMed:21215369, ECO:0000305|PubMed:7961692, ECO:0000305|PubMed:8749392
ChainResidueDetails
ATPO500

site_idSWS_FT_FI13
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P05771
ChainResidueDetails
ATHR504

site_idSWS_FT_FI14
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:21215369, ECO:0000269|PubMed:8327493, ECO:0000269|PubMed:8749392, ECO:0007744|PubMed:22673903
ChainResidueDetails
APRO642

site_idSWS_FT_FI15
Number of Residues1
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:21215369, ECO:0000269|PubMed:8749392
ChainResidueDetails
APHE661

site_idSWS_FT_FI16
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by SYK => ECO:0000250|UniProtKB:P68404
ChainResidueDetails
AVAL662

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PDB entries from 2024-07-24

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