1APO

THREE-DIMENSIONAL STRUCTURE OF THE APO FORM OF THE N-TERMINAL EGF-LIKE MODULE OF BLOOD COAGULATION FACTOR X AS DETERMINED BY NMR SPECTROSCOPY AND SIMULATED FOLDING

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005509	molecular_function	calcium ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE OH A 87

Chain	Residue
A	ASP63
A	GLY64

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	CYS61-CYS72

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

Chain	Residue	Details
A	CYS70-CYS81

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

Chain	Residue	Details
A	CYS70-CYS81

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site_id	PS01187
Number of Residues	25
Details	EGF_CA Calcium-binding EGF-like domain signature. DgDQCeghp..........Clnqgh..CkDgigdYtC

Chain	Residue	Details
A	ASP46-CYS70

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	36
Details	Domain: {"description":"EGF-like 1; calcium-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	1
Details	Modified residue: {"description":"(3R)-3-hydroxyaspartate","evidences":[{"source":"PubMed","id":"6688526","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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