Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1SFC

NEURONAL SYNAPTIC FUSION 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
I	0016020	cellular_component	membrane
I	0016192	biological_process	vesicle-mediated transport
J	0005484	molecular_function	SNAP receptor activity
J	0006886	biological_process	intracellular protein transport
J	0016020	cellular_component	membrane
J	0016192	biological_process	vesicle-mediated transport
K	0000149	molecular_function	SNARE binding
K	0005249	molecular_function	voltage-gated potassium channel activity
K	0017075	molecular_function	syntaxin-1 binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE SR D 288

Chain	Residue
D	HOH516

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SR A 289

Chain	Residue
A	ASP68
A	HOH513
I	SER75
I	GLU78
I	THR79
I	HOH506
I	HOH510

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SR A 290

Chain	Residue
A	GLU78
A	THR79
A	HOH507
I	ASP68
I	MPD930
A	SER75

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SR F 291

Chain	Residue
F	ASP242
F	GLU245
F	HOH504
F	HOH511
J	ASP242
J	GLU245
J	HOH508

site_id	AC5
Number of Residues	1
Details	BINDING SITE FOR RESIDUE SR J 292

Chain	Residue
J	ASP218

site_id	AC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SR K 293

Chain	Residue
G	ASP41
K	GLU37

site_id	AC7
Number of Residues	1
Details	BINDING SITE FOR RESIDUE SR B 294

Chain	Residue
B	ASP218

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SR C 295

Chain	Residue
C	GLU55
C	HOH519

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SR C 296

Chain	Residue
C	ASP51
C	GLU55
C	HOH519

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SR F 297

Chain	Residue
F	ASP214
F	ASP218
F	HOH501

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SR G 298

Chain	Residue
G	ASP51
G	GLU55
G	SR299
G	SR300
K	ASP51
K	GLU55

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SR G 299

Chain	Residue
G	ASP51
G	SR298
K	GLU52
K	GLU55

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SR G 300

Chain	Residue
G	GLU55
G	SR298
K	ASP51
K	GLU55
K	MPD929

site_id	BC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MPD F 926

Chain	Residue
B	ASP231
C	GLU52
C	GLN53
E	GLN71
F	TYR235
F	ASN236

site_id	BC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MPD A 927

Chain	Residue
A	ARG86
A	TRP89
I	ASP57
J	SER225
J	MET229

site_id	BC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MPD A 928

Chain	Residue
A	ASP65
A	ASP68

site_id	BC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MPD K 929

Chain	Residue
G	SR300
K	LYS76
K	ASP80
L	GLU170

site_id	BC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MPD I 930

Chain	Residue
A	GLN76
A	THR79
A	SR290
I	ASP68
I	ALA69

site_id	CC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE MPD K 931

Chain	Residue
K	GLN15

site_id	CC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MPD G 932

Chain	Residue
F	GLU245
G	HIS66
G	GLN69
G	ASP70

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ASN49-ASP68

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

Chain	Residue	Details
B	ARG198-VAL237

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
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
D	ARG180
H	ARG180
L	ARG180

site_id	SWS_FT_FI2
Number of Residues	3
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
D	GLN197
H	GLN197
L	GLN197

site_id	SWS_FT_FI3
Number of Residues	3
Details	MOD_RES: Phosphothreonine; by PKC and PKA => ECO:0000269\|PubMed:12459461

Chain	Residue	Details
D	THR138
J	LYS253
J	LYS256
H	THR138
L	THR138
B	LYS256
F	LYS252
F	LYS253
F	LYS256
J	LYS252

site_id	SWS_FT_FI4
Number of Residues	3
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:P60879

Chain	Residue	Details
D	SER154
H	SER154
L	SER154

site_id	SWS_FT_FI5
Number of Residues	3
Details	MOD_RES: Phosphoserine; by PKC => ECO:0000269\|PubMed:12459461

Chain	Residue	Details
D	SER187
H	SER187
L	SER187

site_id	SWS_FT_FI6
Number of Residues	3
Details	SITE: (Microbial infection) Cleavage; by C.botulinum neurotoxin type G (BoNT/G, botG) => ECO:0000269\|PubMed:7910017

Chain	Residue	Details
A	ALA81
E	ALA81
I	ALA81

site_id	SWS_FT_FI7
Number of Residues	3
Details	MOD_RES: N-acetylserine => ECO:0000250\|UniProtKB:P63026

Chain	Residue	Details
A	SER2
E	SER2
I	SER2

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)