1SPP

THE CRYSTAL STRUCTURES OF TWO MEMBERS OF THE SPERMADHESIN FAMILY REVEAL THE FOLDING OF THE CUB DOMAIN

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005576	cellular_component	extracellular region
A	0007338	biological_process	single fertilization
B	0005576	cellular_component	extracellular region
B	0007338	biological_process	single fertilization

Functional Information from PROSITE/UniProt

site_id	PS00985
Number of Residues	25
Details	SPERMADHESIN_1 Spermadhesins family signature 1. CGgrLtddyGtIftykgpkteCvWT

Chain	Residue	Details
A	CYS9-THR33
B	CYS9-THR33

---

site_id	PS00986
Number of Residues	22
Details	SPERMADHESIN_2 Spermadhesins family signature 2. CgKEyVEVlEgapGskslgKfC

Chain	Residue	Details
A	CYS53-CYS74
B	CYS53-CYS74

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	201
Details	Domain: {"description":"CUB","evidences":[{"source":"PROSITE-ProRule","id":"PRU00059","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","featureId":"CAR_000189","evidences":[{"source":"PubMed","id":"7781775","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","featureId":"CAR_000148","evidences":[{"source":"PubMed","id":"7781775","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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