3TH3

Mg2+ Is Required for Optimal Folding of the Gamma-Carboxyglutamic Acid (Gla) Domains of Vitamin K-Dependent Clotting Factors At Physiological Ca2+

Functional Information from GO Data

Chain	GOid	namespace	contents
H	0004252	molecular_function	serine-type endopeptidase activity
H	0006508	biological_process	proteolysis
L	0005509	molecular_function	calcium ion binding
L	0005576	cellular_component	extracellular region
T	0007596	biological_process	blood coagulation
T	0016020	cellular_component	membrane

Functional Information from PROSITE/UniProt

site_id	PS00010
Number of Residues	12
Details	ASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CkDqlqsYiCfC

Chain	Residue	Details
L	CYS61-CYS72

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site_id	PS00011
Number of Residues	26
Details	GLA_1 Vitamin K-dependent carboxylation domain. EckEEqCsfeearEifkdaertkl.FW

Chain	Residue	Details
L	CGU16-TRP41

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

Chain	Residue	Details
L	CYS70-CYS81

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site_id	PS00134
Number of Residues	6
Details	TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VSAAHC

Chain	Residue	Details
H	VAL53-CYS58

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site_id	PS00135
Number of Residues	12
Details	TRYPSIN_SER Serine proteases, trypsin family, serine active site. DSckGDSGGPHA

Chain	Residue	Details
H	ASP189-ALA200

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site_id	PS00621
Number of Residues	18
Details	TISSUE_FACTOR Tissue factor signature. WKsKCfyTtDTECDLTDE

Chain	Residue	Details
T	TRP45-GLU62

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site_id	PS01186
Number of Residues	16
Details	EGF_2 EGF-like domain signature 2. CrCheGYslladgvsC

Chain	Residue	Details
L	CYS112-CYS127

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site_id	PS01187
Number of Residues	25
Details	EGF_CA Calcium-binding EGF-like domain signature. DgDQCassp..........Cqnggs..CkDqlqsYiC

Chain	Residue	Details
L	ASP46-CYS70

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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:0000255

Chain	Residue	Details
T	ASN124
T	ASN137
H	SER195

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site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
H	ASP189
L	CGU7
L	CGU14
L	CGU16
L	CGU20
L	CGU25
L	CGU26
L	CGU29
L	CGU35

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site_id	SWS_FT_FI3
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19167329, ECO:0000269|PubMed:3264725

Chain	Residue	Details
H	ASN175

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: (3R)-3-hydroxyaspartate => ECO:0000269|PubMed:3264725

Chain	Residue	Details
L	ASP63

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site_id	SWS_FT_FI5
Number of Residues	1
Details	CARBOHYD: O-linked (Xyl...) serine; alternate => ECO:0000269|PubMed:1904059, ECO:0000269|PubMed:2129367, ECO:0000269|PubMed:21949356, ECO:0000269|PubMed:2511201

Chain	Residue	Details
L	SER52

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site_id	SWS_FT_FI6
Number of Residues	1
Details	CARBOHYD: O-linked (Fuc) serine => ECO:0000269|PubMed:1904059, ECO:0000269|PubMed:9023546

Chain	Residue	Details
L	SER60

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