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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

3K72

Structure of integrin alphaX beta2

Functional Information from GO Data
ChainGOidnamespacecontents
A0005178molecular_functionintegrin binding
A0005515molecular_functionprotein binding
A0005886cellular_componentplasma membrane
A0007155biological_processcell adhesion
A0007160biological_processcell-matrix adhesion
A0007229biological_processintegrin-mediated signaling pathway
A0008284biological_processpositive regulation of cell population proliferation
A0008305cellular_componentintegrin complex
A0009887biological_processanimal organ morphogenesis
A0009893biological_processpositive regulation of metabolic process
A0009897cellular_componentexternal side of plasma membrane
A0009986cellular_componentcell surface
A0010628biological_processpositive regulation of gene expression
A0016020cellular_componentmembrane
A0030335biological_processpositive regulation of cell migration
A0030667cellular_componentsecretory granule membrane
A0030971molecular_functionreceptor tyrosine kinase binding
A0031643biological_processpositive regulation of myelination
A0034113biological_processheterotypic cell-cell adhesion
A0034689cellular_componentintegrin alphaX-beta2 complex
A0038023molecular_functionsignaling receptor activity
A0045766biological_processpositive regulation of angiogenesis
A0046872molecular_functionmetal ion binding
A0051607biological_processdefense response to virus
A0070821cellular_componenttertiary granule membrane
A0098609biological_processcell-cell adhesion
A0101003cellular_componentficolin-1-rich granule membrane
A1905956biological_processpositive regulation of endothelial tube morphogenesis
B0001540molecular_functionamyloid-beta binding
B0001774biological_processmicroglial cell activation
B0001851molecular_functioncomplement component C3b binding
B0002523biological_processleukocyte migration involved in inflammatory response
B0005178molecular_functionintegrin binding
B0005515molecular_functionprotein binding
B0005886cellular_componentplasma membrane
B0005925cellular_componentfocal adhesion
B0006898biological_processreceptor-mediated endocytosis
B0006909biological_processphagocytosis
B0006911biological_processphagocytosis, engulfment
B0006915biological_processapoptotic process
B0006954biological_processinflammatory response
B0007155biological_processcell adhesion
B0007159biological_processleukocyte cell-cell adhesion
B0007160biological_processcell-matrix adhesion
B0007229biological_processintegrin-mediated signaling pathway
B0007267biological_processcell-cell signaling
B0008305cellular_componentintegrin complex
B0008360biological_processregulation of cell shape
B0009897cellular_componentexternal side of plasma membrane
B0009986cellular_componentcell surface
B0016020cellular_componentmembrane
B0019901molecular_functionprotein kinase binding
B0030369molecular_functionICAM-3 receptor activity
B0030593biological_processneutrophil chemotaxis
B0031072molecular_functionheat shock protein binding
B0031623biological_processreceptor internalization
B0032930biological_processpositive regulation of superoxide anion generation
B0033627biological_processcell adhesion mediated by integrin
B0034113biological_processheterotypic cell-cell adhesion
B0034687cellular_componentintegrin alphaL-beta2 complex
B0034688cellular_componentintegrin alphaM-beta2 complex
B0034689cellular_componentintegrin alphaX-beta2 complex
B0035579cellular_componentspecific granule membrane
B0035987biological_processendodermal cell differentiation
B0038024molecular_functioncargo receptor activity
B0043113biological_processreceptor clustering
B0043235cellular_componentreceptor complex
B0043315biological_processpositive regulation of neutrophil degranulation
B0043542biological_processendothelial cell migration
B0044853cellular_componentplasma membrane raft
B0044877molecular_functionprotein-containing complex binding
B0045121cellular_componentmembrane raft
B0045123biological_processcellular extravasation
B0045429biological_processpositive regulation of nitric oxide biosynthetic process
B0045766biological_processpositive regulation of angiogenesis
B0045963biological_processnegative regulation of dopamine metabolic process
B0046872molecular_functionmetal ion binding
B0050730biological_processregulation of peptidyl-tyrosine phosphorylation
B0050839molecular_functioncell adhesion molecule binding
B0070062cellular_componentextracellular exosome
B0070821cellular_componenttertiary granule membrane
B0071404biological_processcellular response to low-density lipoprotein particle stimulus
B0090314biological_processpositive regulation of protein targeting to membrane
B0097242biological_processamyloid-beta clearance
B0098609biological_processcell-cell adhesion
B0098742biological_processcell-cell adhesion via plasma-membrane adhesion molecules
B0101003cellular_componentficolin-1-rich granule membrane
B1903561cellular_componentextracellular vesicle
B1904996biological_processpositive regulation of leukocyte adhesion to vascular endothelial cell
B1990266biological_processneutrophil migration
C0005178molecular_functionintegrin binding
C0005515molecular_functionprotein binding
C0005886cellular_componentplasma membrane
C0007155biological_processcell adhesion
C0007160biological_processcell-matrix adhesion
C0007229biological_processintegrin-mediated signaling pathway
C0008284biological_processpositive regulation of cell population proliferation
C0008305cellular_componentintegrin complex
C0009887biological_processanimal organ morphogenesis
C0009893biological_processpositive regulation of metabolic process
C0009897cellular_componentexternal side of plasma membrane
C0009986cellular_componentcell surface
C0010628biological_processpositive regulation of gene expression
C0016020cellular_componentmembrane
C0030335biological_processpositive regulation of cell migration
C0030667cellular_componentsecretory granule membrane
C0030971molecular_functionreceptor tyrosine kinase binding
C0031643biological_processpositive regulation of myelination
C0034113biological_processheterotypic cell-cell adhesion
C0034689cellular_componentintegrin alphaX-beta2 complex
C0038023molecular_functionsignaling receptor activity
C0045766biological_processpositive regulation of angiogenesis
C0046872molecular_functionmetal ion binding
C0051607biological_processdefense response to virus
C0070821cellular_componenttertiary granule membrane
C0098609biological_processcell-cell adhesion
C0101003cellular_componentficolin-1-rich granule membrane
C1905956biological_processpositive regulation of endothelial tube morphogenesis
D0001540molecular_functionamyloid-beta binding
D0001774biological_processmicroglial cell activation
D0001851molecular_functioncomplement component C3b binding
D0002523biological_processleukocyte migration involved in inflammatory response
D0005178molecular_functionintegrin binding
D0005515molecular_functionprotein binding
D0005886cellular_componentplasma membrane
D0005925cellular_componentfocal adhesion
D0006898biological_processreceptor-mediated endocytosis
D0006909biological_processphagocytosis
D0006911biological_processphagocytosis, engulfment
D0006915biological_processapoptotic process
D0006954biological_processinflammatory response
D0007155biological_processcell adhesion
D0007159biological_processleukocyte cell-cell adhesion
D0007160biological_processcell-matrix adhesion
D0007229biological_processintegrin-mediated signaling pathway
D0007267biological_processcell-cell signaling
D0008305cellular_componentintegrin complex
D0008360biological_processregulation of cell shape
D0009897cellular_componentexternal side of plasma membrane
D0009986cellular_componentcell surface
D0016020cellular_componentmembrane
D0019901molecular_functionprotein kinase binding
D0030369molecular_functionICAM-3 receptor activity
D0030593biological_processneutrophil chemotaxis
D0031072molecular_functionheat shock protein binding
D0031623biological_processreceptor internalization
D0032930biological_processpositive regulation of superoxide anion generation
D0033627biological_processcell adhesion mediated by integrin
D0034113biological_processheterotypic cell-cell adhesion
D0034687cellular_componentintegrin alphaL-beta2 complex
D0034688cellular_componentintegrin alphaM-beta2 complex
D0034689cellular_componentintegrin alphaX-beta2 complex
D0035579cellular_componentspecific granule membrane
D0035987biological_processendodermal cell differentiation
D0038024molecular_functioncargo receptor activity
D0043113biological_processreceptor clustering
D0043235cellular_componentreceptor complex
D0043315biological_processpositive regulation of neutrophil degranulation
D0043542biological_processendothelial cell migration
D0044853cellular_componentplasma membrane raft
D0044877molecular_functionprotein-containing complex binding
D0045121cellular_componentmembrane raft
D0045123biological_processcellular extravasation
D0045429biological_processpositive regulation of nitric oxide biosynthetic process
D0045766biological_processpositive regulation of angiogenesis
D0045963biological_processnegative regulation of dopamine metabolic process
D0046872molecular_functionmetal ion binding
D0050730biological_processregulation of peptidyl-tyrosine phosphorylation
D0050839molecular_functioncell adhesion molecule binding
D0070062cellular_componentextracellular exosome
D0070821cellular_componenttertiary granule membrane
D0071404biological_processcellular response to low-density lipoprotein particle stimulus
D0090314biological_processpositive regulation of protein targeting to membrane
D0097242biological_processamyloid-beta clearance
D0098609biological_processcell-cell adhesion
D0098742biological_processcell-cell adhesion via plasma-membrane adhesion molecules
D0101003cellular_componentficolin-1-rich granule membrane
D1903561cellular_componentextracellular vesicle
D1904996biological_processpositive regulation of leukocyte adhesion to vascular endothelial cell
D1990266biological_processneutrophil migration
Functional Information from PROSITE/UniProt
site_idPS00022
Number of Residues12
DetailsEGF_1 EGF-like domain signature 1. CrCdtGyiGKnC
ChainResidueDetails
BCYS448-CYS459
BCYS540-CYS551
site_idPS00243
Number of Residues14
DetailsI_EGF_1 Integrins beta chain EGF (I-EGF) domain signature. CsGl..GdCvCgqClC
ChainResidueDetails
BCYS484-CYS497
BCYS527-CYS542
BCYS568-CYS581
site_idPS01186
Number of Residues14
DetailsEGF_2 EGF-like domain signature 2. CrCdtGYigknce..C
ChainResidueDetails
BCYS448-CYS461
BCYS540-CYS553
BCYS579-CYS593
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues110
DetailsRepeat: {"description":"FG-GAP 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00803","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues118
DetailsRepeat: {"description":"FG-GAP 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00803","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues102
DetailsRepeat: {"description":"FG-GAP 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00803","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues120
DetailsRepeat: {"description":"FG-GAP 5","evidences":[{"source":"PROSITE-ProRule","id":"PRU00803","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues116
DetailsRepeat: {"description":"FG-GAP 6","evidences":[{"source":"PROSITE-ProRule","id":"PRU00803","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues120
DetailsRepeat: {"description":"FG-GAP 7","evidences":[{"source":"PROSITE-ProRule","id":"PRU00803","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues22
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P08648","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues8
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"20033057","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues10
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20033057","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues100
DetailsDomain: {"description":"PSI","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues478
DetailsDomain: {"description":"VWFA","evidences":[{"source":"UniProtKB","id":"P05106","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues66
DetailsDomain: {"description":"I-EGF 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01392","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues104
DetailsDomain: {"description":"I-EGF 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU01392","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues76
DetailsDomain: {"description":"I-EGF 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU01392","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues76
DetailsDomain: {"description":"I-EGF 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU01392","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues4
DetailsMotif: {"description":"Cell attachment site","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues6
DetailsBinding site: {"description":"in MIDAS binding site","evidences":[{"source":"PubMed","id":"24385486","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4NEH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4NEN","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues2
DetailsBinding site: {"description":"in ADMIDAS binding site","evidences":[{"source":"PubMed","id":"20033057","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3K6S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3K71","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3K72","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues2
DetailsBinding site: {"description":"in ADMIDAS binding site","evidences":[{"source":"PubMed","id":"20033057","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24385486","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3K6S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3K71","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3K72","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4NEH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4NEN","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues8
DetailsBinding site: {"description":"in LIMBS binding site","evidences":[{"source":"PubMed","id":"24385486","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4NEH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4NEN","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues2
DetailsBinding site: {"description":"in ADMIDAS binding site and liganded-open conformation","evidences":[{"source":"PubMed","id":"24385486","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4NEN","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues2
DetailsBinding site: {"description":"in ADMIDAS binding site and unliganded-closed conformation","evidences":[{"source":"PubMed","id":"20033057","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24385486","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3K6S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3K71","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3K72","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4NEH","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues2
DetailsModified residue: {"description":"Pyrrolidone carboxylic acid","evidences":[{"source":"PubMed","id":"2954816","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19349973","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19349973","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20033057","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24385486","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4NEH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4NEN","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19349973","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI28
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"24385486","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4NEH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4NEN","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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