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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8GMB

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
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
A0002376biological_processimmune system process
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
A0006351biological_processDNA-templated transcription
A0006468biological_processprotein phosphorylation
A0006915biological_processapoptotic process
A0008270molecular_functionzinc ion binding
A0008289molecular_functionlipid binding
A0016004molecular_functionphospholipase activator activity
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0018108biological_processpeptidyl-tyrosine phosphorylation
A0030167biological_processproteoglycan catabolic process
A0030889biological_processnegative regulation of B cell proliferation
A0030890biological_processpositive regulation of B cell proliferation
A0031410cellular_componentcytoplasmic vesicle
A0032481biological_processpositive regulation of type I interferon production
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
A0038083biological_processpeptidyl-tyrosine autophosphorylation
A0042113biological_processB cell activation
A0042802molecular_functionidentical protein binding
A0043274molecular_functionphospholipase binding
A0045087biological_processinnate immune response
A0045121cellular_componentmembrane raft
A0046777biological_processprotein autophosphorylation
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
A0050864biological_processregulation of B cell activation
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
A0140896biological_processcGAS/STING signaling pathway
A0141111biological_processpositive regulation of cGAS/STING signaling pathway
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 Residues60
DetailsDomain: {"description":"SH3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00192","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues253
DetailsDomain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues7
DetailsMotif: {"description":"CAV1-binding","evidences":[{"source":"UniProtKB","id":"Q06187","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10028","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"8630736","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"17947660","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q06187","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine; by LYN and SYK","evidences":[{"source":"PubMed","id":"8629002","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17947660","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues3
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q06187","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

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PDB entries from 2026-01-21

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