1D3L

D1D2-ICAM-1 FULLY GLYCOSYLATED, VARIATION OF D1-D2 INTERDOMAIN ANGLE IN DIFFERENT CRYSTAL STRUCTURES.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005178	molecular_function	integrin binding
A	0007155	biological_process	cell adhesion
A	0016020	cellular_component	membrane
A	0098609	biological_process	cell-cell adhesion

Functional Information from PDB Data

site_id	GS1
Number of Residues	1
Details	N-GLYCOSYLATION SITE

Chain	Residue
A	ASN103

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site_id	GS2
Number of Residues	1
Details	N-GLYCOSYLATION SITE

Chain	Residue
A	ASN118

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site_id	GS3
Number of Residues	1
Details	N-GLYCOSYLATION SITE

Chain	Residue
A	ASN156

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site_id	GS4
Number of Residues	1
Details	N-GLYCOSYLATION SITE

Chain	Residue
A	ASN175

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12526797, ECO:0000269|PubMed:9539702

Chain	Residue	Details
A	ASN103
A	ASN156

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site_id	SWS_FT_FI2
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:12526797, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:9539702

Chain	Residue	Details
A	ASN118

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site_id	SWS_FT_FI3
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12526797, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:9539702, ECO:0000269|PubMed:9539703

Chain	Residue	Details
A	ASN175

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