Structure of PDB 7usm Chain A

Receptor sequence
>7usmA (length=848) Species: 9606 (Homo sapiens) [Search protein sequence]
FNLDTENAMTFQENARGFGQSVVQLQGSRVVVGAPQEIVAANQRGSLYQC
DYSTGSCEPIRLQVPVEAVNMSLGLSLAATTSPPQLLACGPTVHQTCSEN
TYVKGLCFLFGSNLRQQPQKHEMSQEGFSAAITSNGPLLSTVGSYDWAGG
VFLYTSKEKSTFINMTRVDSDMNDAYLGYAAAIILRNRVQSLVLGAPRYQ
HIGLVAMFRQNTGMWESNANVKGTQIGAYFGASLCSVDVDSNGSTDLVLI
GAPHYYEQTRGGQVSVCPLPRGRARWQCDAVLYGEQGQPWGRFGAALTVL
GDVNGDKLTDVAIGAPGEEDNRGAVYLFHGTSGSGISPSHSQRIAGSKLS
PRLQYFGQSLSGGQDLTMDGLVDLTVGAQGHVLLLRSQPVLRVKAIMEFN
PREVARNVFECGKEAGEVRVCLHVQKSTRDRLREGQIQSVVTYDLALDSG
RPHSRAVFNETKNSTRRQTQVLGLTQTCETLKLQLPNCIEDPVSPIVLRL
NFSLVGTPLSAFGNLRPVLAEDAQRLFTALFPFEKNCGNDNICQDDLSIT
FSFMSLDCLVVGGPREFNVTVTVRNDGEDSYRTQVTFFFPLDLSYRKVST
WRLACESLKSTSCSINHPIFPENSEVTFNITFDVDSKASLGNKLLLKANV
TSENNMPRTNKTEFQLELPVKYAVYMVVTSHGVSTKYLNFTASENTSRVM
QHQYQVSNLGQRSLPISLVFLVPVRLNQTVIWDRPQVTFSENLSSTCHTK
ERLPSHSDFLAELRKAPVVNCSIAVCQRIQCDIPFFGIQEEFNATLKGNL
SFDWYIKTSHNHLLIVSTAEILFNDSVFTLLPGQGAFVRSQTETKVEP
3D structure
PDB7usm Structural basis for non-canonical integrin engagement by Bordetella adenylate cyclase toxin.
ChainA
Resolution2.7 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Enzyme Commision number ?
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 CA A D576 T578 D580 L582 D584 D365 T367 D369 L371 D373
BS02 CA A D513 N515 D517 L519 D521 D302 N304 D306 L308 D310
BS03 CA A D451 N453 S455 D457 D240 N242 S244 D246
Gene Ontology
Molecular Function
GO:0001540 amyloid-beta binding
GO:0001851 complement component C3b binding
GO:0005178 integrin binding
GO:0005515 protein binding
GO:0031072 heat shock protein binding
GO:0038024 cargo receptor activity
GO:0044877 protein-containing complex binding
GO:0046872 metal ion binding
Biological Process
GO:0001774 microglial cell activation
GO:0002430 complement receptor mediated signaling pathway
GO:0002931 response to ischemia
GO:0006898 receptor-mediated endocytosis
GO:0006911 phagocytosis, engulfment
GO:0007155 cell adhesion
GO:0007160 cell-matrix adhesion
GO:0007229 integrin-mediated signaling pathway
GO:0009612 response to mechanical stimulus
GO:0010668 ectodermal cell differentiation
GO:0030900 forebrain development
GO:0032355 response to estradiol
GO:0032930 positive regulation of superoxide anion generation
GO:0033627 cell adhesion mediated by integrin
GO:0034113 heterotypic cell-cell adhesion
GO:0043315 positive regulation of neutrophil degranulation
GO:0045087 innate immune response
GO:0045963 negative regulation of dopamine metabolic process
GO:0090314 positive regulation of protein targeting to membrane
GO:0097242 amyloid-beta clearance
GO:0098609 cell-cell adhesion
GO:0098742 cell-cell adhesion via plasma-membrane adhesion molecules
GO:0140459 response to Gram-positive bacterium
GO:0150062 complement-mediated synapse pruning
GO:0150064 vertebrate eye-specific patterning
GO:1904151 positive regulation of microglial cell mediated cytotoxicity
GO:1904643 response to curcumin
GO:2000363 positive regulation of prostaglandin-E synthase activity
Cellular Component
GO:0005615 extracellular space
GO:0005886 plasma membrane
GO:0008305 integrin complex
GO:0009897 external side of plasma membrane
GO:0009986 cell surface
GO:0034688 integrin alphaM-beta2 complex
GO:0035579 specific granule membrane
GO:0044853 plasma membrane raft
GO:0045121 membrane raft
GO:0070062 extracellular exosome
GO:0070821 tertiary granule membrane

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:7usm, PDBe:7usm, PDBj:7usm
PDBsum7usm
PubMed35977491
UniProtP11215|ITAM_HUMAN Integrin alpha-M (Gene Name=ITGAM)

[Back to BioLiP]