Structure of PDB 8gmb Chain A

Receptor sequence
>8gmbA (length=438) Species: 10090 (Mus musculus) [Search protein sequence]
TELKKVVALYDYMPMNANDLQLRKGEEYFILEESNLPWWRARDKNGQEGY
IPSNYITEAEDSIEMYEWYSKHMTRSQAEQLLKQAGGGFIVRDSKYTVSV
FAKGEPQGVIRHYVVCSTPQSQYYLAEKHLFSTIPELINYHQHNSAGLIS
RLKYPVSKQNKNPPPPPGFGYGSWEIDPKDLTFLKELGTGQFGVVKYGKW
RGQYDVAIRMIREGSMSEDEFIEEAKVMMNLSHEKLVQLYGVCTKQRPIF
IITEYMANGCLLNYLREMRHRFQTQQLLEMCKDVCEAMEYLESKQFLHRD
LAARNCLVNDQGVVKVSDFGMTRYVLDDEYTSSTGSKFPVKWASPEVLMY
SKFSSKSDIWAFGVLMWEIYSLGKMPYERFTNSETAEHIAQGLRLPRPHL
ASERVYTIMYSCWHEKADERPSFKILLSNILDVMDEES
3D structure
PDB8gmb Crystal structure of full-length Bruton's Tryrosine Kinase
ChainA
Resolution3.4 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.7.10.2: non-specific protein-tyrosine kinase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 9AJ A L408 T410 G411 Q412 V416 R430 Y476 M477 A478 G480 L528 D539 Y551 L187 T189 G190 Q191 V195 R209 Y255 M256 A257 G259 L307 D318 Y330
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004713 protein tyrosine kinase activity
GO:0004715 non-membrane spanning protein tyrosine kinase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0005547 phosphatidylinositol-3,4,5-trisphosphate binding
GO:0008289 lipid binding
GO:0016004 phospholipase activator activity
GO:0042802 identical protein binding
GO:0043274 phospholipase binding
GO:0046872 metal ion binding
Biological Process
GO:0001780 neutrophil homeostasis
GO:0001805 positive regulation of type III hypersensitivity
GO:0001812 positive regulation of type I hypersensitivity
GO:0001818 negative regulation of cytokine production
GO:0002250 adaptive immune response
GO:0002344 B cell affinity maturation
GO:0002553 histamine secretion by mast cell
GO:0002639 positive regulation of immunoglobulin production
GO:0006468 protein phosphorylation
GO:0006915 apoptotic process
GO:0016310 phosphorylation
GO:0018108 peptidyl-tyrosine phosphorylation
GO:0030167 proteoglycan catabolic process
GO:0030889 negative regulation of B cell proliferation
GO:0030890 positive regulation of B cell proliferation
GO:0032496 response to lipopolysaccharide
GO:0032693 negative regulation of interleukin-10 production
GO:0032755 positive regulation of interleukin-6 production
GO:0032760 positive regulation of tumor necrosis factor production
GO:0034614 cellular response to reactive oxygen species
GO:0035556 intracellular signal transduction
GO:0045087 innate immune response
GO:0048469 cell maturation
GO:0050766 positive regulation of phagocytosis
GO:0050853 B cell receptor signaling pathway
GO:0050869 negative regulation of B cell activation
GO:0061516 monocyte proliferation
GO:0070664 negative regulation of leukocyte proliferation
GO:0071226 cellular response to molecule of fungal origin
GO:0098761 cellular response to interleukin-7
GO:0150153 positive regulation of interleukin-17A production
GO:1900227 positive regulation of NLRP3 inflammasome complex assembly
GO:1901647 positive regulation of synoviocyte proliferation
GO:1990959 eosinophil homeostasis
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0031410 cytoplasmic vesicle
GO:0045121 membrane raft
GO:0048471 perinuclear region of cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:8gmb, PDBe:8gmb, PDBj:8gmb
PDBsum8gmb
PubMed38189455
UniProtP35991|BTK_MOUSE Tyrosine-protein kinase BTK (Gene Name=Btk)

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