8OS5

Crystal structure of the Factor XII heavy chain reveals an interlocking dimer with a FnII to kringle domain interaction

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005509	molecular_function	calcium ion binding
A	0005576	cellular_component	extracellular region
B	0005509	molecular_function	calcium ion binding
B	0005576	cellular_component	extracellular region
C	0005509	molecular_function	calcium ion binding
C	0005576	cellular_component	extracellular region

Functional Information from PROSITE/UniProt

site_id	PS00021
Number of Residues	13
Details	KRINGLE_1 Kringle domain signature. FCRNpdndirp.WC

Chain	Residue	Details
A	PHE246-CYS258

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

Chain	Residue	Details
A	CYS100-CYS111
A	CYS179-CYS190

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site_id	PS00023
Number of Residues	42
Details	FN2_1 Fibronectin type-II collagen-binding domain signature. ChfPFqYhrqlyhkCthkgrpgpqpWCattpNFdqdqrWgYC

Chain	Residue	Details
A	CYS28-CYS69

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

Chain	Residue	Details
A	CYS179-CYS190

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site_id	PS01253
Number of Residues	36
Details	FN1_1 Fibronectin type-I domain signature. CfepqllrfFhkneiWyRteqaavar..CqCkgpdah...C

Chain	Residue	Details
A	CYS116-CYS151

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	CARBOHYD: O-linked (Fuc) threonine => ECO:0000269|PubMed:1544894

Chain	Residue	Details
A	THR90
B	THR90
C	THR90

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site_id	SWS_FT_FI2
Number of Residues	3
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:3877053, ECO:0000269|PubMed:3886654

Chain	Residue	Details
A	ASN230
B	ASN230
C	ASN230

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site_id	SWS_FT_FI3
Number of Residues	6
Details	CARBOHYD: O-linked (GalNAc...) threonine => ECO:0000269|PubMed:3886654

Chain	Residue	Details
A	THR280
A	THR286
B	THR280
B	THR286
C	THR280
C	THR286

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site_id	SWS_FT_FI4
Number of Residues	3
Details	CARBOHYD: O-linked (GalNAc...) serine => ECO:0000269|PubMed:3886654

Chain	Residue	Details
A	SER289
B	SER289
C	SER289

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