3DEM

CUB1-EGF-CUB2 domain of HUMAN MASP-1/3

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005509	molecular_function	calcium ion binding
B	0005509	molecular_function	calcium ion binding

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	CYS138-CYS149

---

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

Chain	Residue	Details
A	CYS147-CYS162

---

site_id	PS01187
Number of Residues	28
Details	EGF_CA Calcium-binding EGF-like domain signature. DvDECkeredeels.....Cdhy....ChNyiggYyC

Chain	Residue	Details
A	ASP120-CYS147

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	224
Details	Domain: {"description":"CUB 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00059","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	28
Details	Binding site: {}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Modified residue: {"description":"(3R)-3-hydroxyasparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"11290788","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18596036","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19139490","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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