6WVW

Crystal structure of the R59P-SNAP25 containing SNARE complex

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
E	0016192	biological_process	vesicle-mediated transport
F	0005484	molecular_function	SNAP receptor activity
F	0006886	biological_process	intracellular protein transport
F	0016020	cellular_component	membrane
F	0016192	biological_process	vesicle-mediated transport
G	0000149	molecular_function	SNARE binding
G	0005249	molecular_function	voltage-gated potassium channel activity
G	0017075	molecular_function	syntaxin-1 binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	binding site for residue CA B 301

Chain	Residue
B	GLU238
B	HOH401

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site_id	AC2
Number of Residues	3
Details	binding site for residue MPD C 201

Chain	Residue
C	ARG30
C	LEU33
C	GLN34

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site_id	AC3
Number of Residues	5
Details	binding site for residue CA C 202

Chain	Residue
D	HOH343
C	GLY54
C	ASP58
C	HOH314
D	GLN177

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site_id	AC4
Number of Residues	2
Details	binding site for residue MPD E 101

Chain	Residue
E	LYS83
E	HOH202

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site_id	AC5
Number of Residues	4
Details	binding site for residue CA E 102

Chain	Residue
D	HOH323
E	ASP65
E	HOH210
E	HOH227

---

site_id	AC6
Number of Residues	3
Details	binding site for residue CA F 301

Chain	Residue
F	GLU238
F	HOH403
F	HOH427

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ASN49-ASP68

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	SITE: (Microbial infection) Cleavage; by C.botulinum neurotoxin type E (BoNT/E) => ECO:0000269|PubMed:8243676, ECO:0000269|PubMed:8294407, ECO:0000305|PubMed:8103915

Chain	Residue	Details
H	ARG180
D	ARG180

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site_id	SWS_FT_FI2
Number of Residues	2
Details	SITE: (Microbial infection) Cleavage; by C.botulinum neurotoxin type A (BoNT/A, botA) => ECO:0000269|PubMed:8243676, ECO:0000269|PubMed:8294407, ECO:0000305|PubMed:8103915

Chain	Residue	Details
B	LYS256
F	LYS252
F	LYS253
F	LYS256
D	GLN197
H	GLN197
B	LYS253

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P60879

Chain	Residue	Details
H	SER154
D	SER154

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site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Phosphoserine; by PKC => ECO:0000269|PubMed:12459461

Chain	Residue	Details
H	SER187
D	SER187

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site_id	SWS_FT_FI5
Number of Residues	2
Details	SITE: (Microbial infection) Cleavage; by C.botulinum neurotoxin type G (BoNT/G, botG) => ECO:0000269|PubMed:7910017

Chain	Residue	Details
E	ALA81
A	ALA81

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