4QD2

Molecular basis for disruption of E-cadherin adhesion by botulinum neurotoxin A complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005576	cellular_component	extracellular region
B	0005515	molecular_function	protein binding
C	0005515	molecular_function	protein binding
D	0005515	molecular_function	protein binding
E	0005509	molecular_function	calcium ion binding
E	0005886	cellular_component	plasma membrane
E	0007155	biological_process	cell adhesion
E	0007156	biological_process	homophilic cell-cell adhesion
E	0016020	cellular_component	membrane
E	0098609	biological_process	cell-cell adhesion
F	0005576	cellular_component	extracellular region
G	0005515	molecular_function	protein binding
H	0005515	molecular_function	protein binding
I	0005515	molecular_function	protein binding
J	0005509	molecular_function	calcium ion binding
J	0005886	cellular_component	plasma membrane
J	0007155	biological_process	cell adhesion
J	0007156	biological_process	homophilic cell-cell adhesion
J	0016020	cellular_component	membrane
J	0098609	biological_process	cell-cell adhesion

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA E 301

Chain	Residue
E	GLU11
E	ASP67
E	GLU69
E	ASP103
E	HOH417
E	HOH430

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site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA E 302

Chain	Residue
E	GLN101
E	ASP103
E	ASP136
E	GLU11
E	GLU69
E	ASP100

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA E 303

Chain	Residue
E	ASN102
E	ASN104
E	ASP134
E	ASP136
E	ASN143
E	ASP195

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site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA J 301

Chain	Residue
J	GLU11
J	ASP67
J	GLU69
J	ASP103

---

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CA J 302

Chain	Residue
J	GLU11
J	GLU69
J	ASP100
J	GLN101
J	ASP103
J	ASN104
J	ASP136

---

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA J 303

Chain	Residue
J	ASN102
J	ASN104
J	ASP134
J	ASP136
J	ASN143
J	ASP195

---

Functional Information from PROSITE/UniProt

site_id	PS00232
Number of Residues	11
Details	CADHERIN_1 Cadherin domain signature. ItVtDqNDNrP

Chain	Residue	Details
E	ILE96-PRO106

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	4
Details	Glycosylation: {"description":"O-linked (Man...) serine","evidences":[{"source":"PubMed","id":"28973932","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Glycosylation: {"description":"O-linked (Man...) threonine","evidences":[{"source":"PubMed","id":"28973932","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---