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7USM

Integrin alphaM/beta2 ectodomain

Functional Information from GO Data
ChainGOidnamespacecontents
A0001540molecular_functionamyloid-beta binding
A0001774biological_processmicroglial cell activation
A0001851molecular_functioncomplement component C3b binding
A0002430biological_processcomplement receptor mediated signaling pathway
A0002931biological_processresponse to ischemia
A0005178molecular_functionintegrin binding
A0005515molecular_functionprotein binding
A0005615cellular_componentextracellular space
A0005886cellular_componentplasma membrane
A0006898biological_processreceptor-mediated endocytosis
A0006911biological_processphagocytosis, engulfment
A0007155biological_processcell adhesion
A0007160biological_processcell-matrix adhesion
A0007229biological_processintegrin-mediated signaling pathway
A0008305cellular_componentintegrin complex
A0009612biological_processresponse to mechanical stimulus
A0009897cellular_componentexternal side of plasma membrane
A0009986cellular_componentcell surface
A0010668biological_processectodermal cell differentiation
A0030900biological_processforebrain development
A0031072molecular_functionheat shock protein binding
A0032355biological_processresponse to estradiol
A0032930biological_processpositive regulation of superoxide anion generation
A0033627biological_processcell adhesion mediated by integrin
A0034113biological_processheterotypic cell-cell adhesion
A0034688cellular_componentintegrin alphaM-beta2 complex
A0035579cellular_componentspecific granule membrane
A0038024molecular_functioncargo receptor activity
A0043315biological_processpositive regulation of neutrophil degranulation
A0044853cellular_componentplasma membrane raft
A0044877molecular_functionprotein-containing complex binding
A0045087biological_processinnate immune response
A0045121cellular_componentmembrane raft
A0045963biological_processnegative regulation of dopamine metabolic process
A0046872molecular_functionmetal ion binding
A0070062cellular_componentextracellular exosome
A0070821cellular_componenttertiary granule membrane
A0090314biological_processpositive regulation of protein targeting to membrane
A0097242biological_processamyloid-beta clearance
A0098609biological_processcell-cell adhesion
A0098742biological_processcell-cell adhesion via plasma-membrane adhesion molecules
A0140459biological_processresponse to Gram-positive bacterium
A0150062biological_processcomplement-mediated synapse pruning
A0150064biological_processvertebrate eye-specific patterning
A1904151biological_processpositive regulation of microglial cell mediated cytotoxicity
A1904643biological_processresponse to curcumin
A2000363biological_processpositive regulation of prostaglandin-E synthase activity
B0001540molecular_functionamyloid-beta binding
B0001774biological_processmicroglial cell activation
B0001851molecular_functioncomplement component C3b binding
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
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
B0044853cellular_componentplasma membrane raft
B0045121cellular_componentmembrane raft
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
B2000363biological_processpositive regulation of prostaglandin-E synthase activity
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
DetailsINTEGRIN_BETA Integrins beta chain cysteine-rich 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 Residues3
DetailsBINDING: in MIDAS binding site => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
ChainResidueDetails
BSER114
BSER116
BGLU212

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: in ADMIDAS binding site => ECO:0000269|PubMed:20033057, ECO:0007744|PDB:3K6S, ECO:0007744|PDB:3K71, ECO:0007744|PDB:3K72
ChainResidueDetails
BASP119
AASP580
AASP584
AASP451
AASN453
AASP457
AASP513
AASN515
AASP517
AASP521
AASP576

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: in ADMIDAS binding site => ECO:0000269|PubMed:20033057, ECO:0000269|PubMed:24385486, ECO:0007744|PDB:3K6S, ECO:0007744|PDB:3K71, ECO:0007744|PDB:3K72, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
ChainResidueDetails
BASP120
AASN895
AASN962
AASN977
AASN1005
AASN1028
AASN1034
AASN1059
AASN224
AASN375
AASN453
AASN676
AASN680
AASN718
AASN785
AASN864

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: in LIMBS binding site => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
ChainResidueDetails
BASP151
BASN207
BASP209
BPRO211

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: in ADMIDAS binding site and liganded-open conformation => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEN
ChainResidueDetails
BASP242

site_idSWS_FT_FI6
Number of Residues1
DetailsBINDING: in ADMIDAS binding site and unliganded-closed conformation => ECO:0000269|PubMed:20033057, ECO:0000269|PubMed:24385486, ECO:0007744|PDB:3K6S, ECO:0007744|PDB:3K71, ECO:0007744|PDB:3K72, ECO:0007744|PDB:4NEH
ChainResidueDetails
BGLU325

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Pyrrolidone carboxylic acid => ECO:0000305|PubMed:2954816
ChainResidueDetails
BGLN1

site_idSWS_FT_FI8
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973
ChainResidueDetails
BASN28

site_idSWS_FT_FI9
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:20033057, ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
ChainResidueDetails
BASN94

site_idSWS_FT_FI10
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973
ChainResidueDetails
BASN190

site_idSWS_FT_FI11
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
BASN232
BASN479

site_idSWS_FT_FI12
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:24385486, ECO:0007744|PDB:4NEH, ECO:0007744|PDB:4NEN
ChainResidueDetails
BASN620

222036

PDB entries from 2024-07-03

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