5E6V

Re-refinement of the Crystal Structure of the Plexin-Semaphorin-Integrin Domain/Hybrid Domain/I-EGF1 Segment from the Human Integrin b2 Subunit

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0007155	biological_process	cell adhesion
A	0007160	biological_process	cell-matrix adhesion
A	0007229	biological_process	integrin-mediated signaling pathway
A	0008305	cellular_component	integrin complex
A	0038023	molecular_function	signaling receptor activity

Functional Information from PROSITE/UniProt

site_id	PS00022
Number of Residues	12
Details	EGF_1 EGF-like domain signature 1. CrCdtGyiGKnC

Chain	Residue	Details
A	CYS448-CYS459

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site_id	PS01186
Number of Residues	12
Details	EGF_2 EGF-like domain signature 2. CrCdtGYigkn....C

Chain	Residue	Details
A	CYS448-CYS459

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	50
Details	Domain: {"description":"PSI","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	2
Details	Motif: {"description":"Cell attachment site","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19349973","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	1
Details	Glycosylation: {"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"}]}

Chain

Residue

Details

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