3B3Q

Crystal structure of a synaptic adhesion complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0016020	cellular_component	membrane
A	0042043	molecular_function	neurexin family protein binding
B	0016020	cellular_component	membrane
B	0042043	molecular_function	neurexin family protein binding

Functional Information from PROSITE/UniProt

site_id	PS00941
Number of Residues	11
Details	CARBOXYLESTERASE_B_2 Carboxylesterases type-B signature 2. EDCLYLNIYvP

Chain	Residue	Details
A	GLU151-PRO161

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"18084303","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"18084303","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18084303","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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