2N1T

Dynamic binding mode of a synaptotagmin-1-SNARE complex in solution

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0016020	cellular_component	membrane
A	0016192	biological_process	vesicle-mediated transport
B	0005484	molecular_function	SNAP receptor activity
B	0006886	biological_process	intracellular protein transport
B	0016020	cellular_component	membrane
B	0016192	biological_process	vesicle-mediated transport
C	0000149	molecular_function	SNARE binding
C	0005249	molecular_function	voltage-gated potassium channel activity
C	0017075	molecular_function	syntaxin-1 binding
E	0016020	cellular_component	membrane

Functional Information from PROSITE/UniProt

site_id	PS00417
Number of Residues	20
Details	SYNAPTOBREVIN Synaptobrevin signature. NVDKVlERdqKLSeLdDRAD

Chain	Residue	Details
A	ASN49-ASP68

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site_id	PS00914
Number of Residues	40
Details	SYNTAXIN Syntaxin / epimorphin family signature. RhseIikLEnsIrELhdMFmdMamlVesQGemIDrIEyn.V

Chain	Residue	Details
B	ARG198-VAL237

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	5
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00041

Chain	Residue	Details
E	ASP303
E	ASP309
E	ASP363
E	ASP365
E	ASP371

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site_id	SWS_FT_FI2
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P21707

Chain	Residue	Details
E	SER342
E	SER344

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site_id	SWS_FT_FI3
Number of Residues	1
Details	SITE: (Microbial infection) Cleavage; by C.botulinum neurotoxin type C (BoNT/C) => ECO:0000269|PubMed:9886085, ECO:0000305|PubMed:15592454

Chain	Residue	Details
D	ARG198
B	LYS253
B	LYS256

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P60879

Chain	Residue	Details
D	THR138

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site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P60879

Chain	Residue	Details
D	SER154
D	SER187

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