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8GMB

Crystal structure of the full-length Bruton's tyrosine kinase (PH-TH domain not visible)

Functional Information from GO Data
ChainGOidnamespacecontents
A0001780biological_processneutrophil homeostasis
A0001805biological_processpositive regulation of type III hypersensitivity
A0001812biological_processpositive regulation of type I hypersensitivity
A0001818biological_processnegative regulation of cytokine production
A0002250biological_processadaptive immune response
A0002344biological_processB cell affinity maturation
A0002553biological_processhistamine secretion by mast cell
A0002639biological_processpositive regulation of immunoglobulin production
A0004672molecular_functionprotein kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0004715molecular_functionnon-membrane spanning protein tyrosine kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005547molecular_functionphosphatidylinositol-3,4,5-trisphosphate binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006468biological_processprotein phosphorylation
A0006915biological_processapoptotic process
A0008289molecular_functionlipid binding
A0010033biological_processresponse to organic substance
A0016004molecular_functionphospholipase activator activity
A0030167biological_processproteoglycan catabolic process
A0030889biological_processnegative regulation of B cell proliferation
A0030890biological_processpositive regulation of B cell proliferation
A0031410cellular_componentcytoplasmic vesicle
A0032496biological_processresponse to lipopolysaccharide
A0032693biological_processnegative regulation of interleukin-10 production
A0032755biological_processpositive regulation of interleukin-6 production
A0032760biological_processpositive regulation of tumor necrosis factor production
A0034614biological_processcellular response to reactive oxygen species
A0035556biological_processintracellular signal transduction
A0042802molecular_functionidentical protein binding
A0043274molecular_functionphospholipase binding
A0045087biological_processinnate immune response
A0045121cellular_componentmembrane raft
A0046872molecular_functionmetal ion binding
A0048469biological_processcell maturation
A0048471cellular_componentperinuclear region of cytoplasm
A0050766biological_processpositive regulation of phagocytosis
A0050852biological_processT cell receptor signaling pathway
A0050853biological_processB cell receptor signaling pathway
A0050869biological_processnegative regulation of B cell activation
A0061516biological_processmonocyte proliferation
A0070664biological_processnegative regulation of leukocyte proliferation
A0071226biological_processcellular response to molecule of fungal origin
A0098761biological_processcellular response to interleukin-7
A0150153biological_processpositive regulation of interleukin-17A production
A1900227biological_processpositive regulation of NLRP3 inflammasome complex assembly
A1901647biological_processpositive regulation of synoviocyte proliferation
A1990959biological_processeosinophil homeostasis
Functional Information from PROSITE/UniProt
site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FLHrDLAARNCLV
ChainResidueDetails
APHE517-VAL529

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues36
DetailsZN_FING: Btk-type => ECO:0000255|PROSITE-ProRule:PRU00432
ChainResidueDetails
AASN135-ARG171

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028
ChainResidueDetails
AASP521

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q06187
ChainResidueDetails
ALYS26
AARG28
ATYR39
ALYS53

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00432
ChainResidueDetails
AHIS143
ACYS154
ACYS155
ACYS165

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU408
AARG430

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000250|UniProtKB:Q06187
ChainResidueDetails
AALA2

site_idSWS_FT_FI7
Number of Residues6
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q06187
ChainResidueDetails
ASER21
ASER55
ASER115
ASER604
ASER623
ASER659

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:17947660
ChainResidueDetails
ATYR40
ATYR344

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PKC/PRKCB => ECO:0000250|UniProtKB:Q06187
ChainResidueDetails
ASER180

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q06187
ChainResidueDetails
ATHR191

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:8630736
ChainResidueDetails
ATYR223

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q06187
ChainResidueDetails
ATYR361
APRO617

site_idSWS_FT_FI13
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by LYN and SYK => ECO:0000269|PubMed:8629002, ECO:0007744|PubMed:17947660
ChainResidueDetails
ATYR551

220472

PDB entries from 2024-05-29

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