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2P28

Structure of the PHE2 and PHE3 fragments of the integrin beta2 subunit

Functional Information from GO Data
ChainGOidnamespacecontents
A0007155biological_processcell adhesion
A0007160biological_processcell-matrix adhesion
A0007229biological_processintegrin-mediated signaling pathway
A0008305cellular_componentintegrin complex
A0038023molecular_functionsignaling receptor activity
B0007155biological_processcell adhesion
B0007160biological_processcell-matrix adhesion
B0007229biological_processintegrin-mediated signaling pathway
B0008305cellular_componentintegrin complex
B0038023molecular_functionsignaling receptor 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

site_idPS01186
Number of Residues14
DetailsEGF_2 EGF-like domain signature 2. CrCdtGYigknce..C
ChainResidueDetails
BCYS448-CYS461
BCYS540-CYS551

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
BASN479

site_idSWS_FT_FI2
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973
ChainResidueDetails
AASN28

site_idSWS_FT_FI3
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
AASN94

218853

PDB entries from 2024-04-24

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