Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5KJ7

Structure of the Ca2+-bound synaptotagmin-1 SNARE complex (long unit cell form) - from XFEL diffraction

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	1
Details	binding site for residue CA A 101

Chain	Residue
A	GLU55

site_id	AC2
Number of Residues	1
Details	binding site for residue CA A 102

Chain	Residue
A	LYS59

site_id	AC3
Number of Residues	2
Details	binding site for residue CA C 101

Chain	Residue
C	GLY54
D	GLN177

site_id	AC4
Number of Residues	2
Details	binding site for residue CA C 102

Chain	Residue
C	ASP58
C	GLU61

site_id	AC5
Number of Residues	5
Details	binding site for residue CA E 501

Chain	Residue
E	TYR364
E	ASP365
E	ASP303
E	ASP309
E	ASP363

site_id	AC6
Number of Residues	4
Details	binding site for residue CA E 502

Chain	Residue
E	ASP172
E	ASP230
E	PHE231
E	ASP232

site_id	AC7
Number of Residues	2
Details	binding site for residue CA E 503

Chain	Residue
E	ASP172
E	ASP178

site_id	AC8
Number of Residues	4
Details	binding site for residue CA E 504

Chain	Residue
E	MET302
E	ASP303
E	ASP363
E	ASP365

site_id	AC9
Number of Residues	5
Details	binding site for residue CA F 501

Chain	Residue
F	ASP172
F	ASP178
F	ASP230
F	PHE231
F	ASP232

site_id	AD1
Number of Residues	4
Details	binding site for residue CA F 502

Chain	Residue
F	ASP172
F	ASP230
F	ASP232
F	LYS324

site_id	AD2
Number of Residues	3
Details	binding site for residue CA F 503

Chain	Residue
F	ASP303
F	ASP309
F	TYR364

site_id	AD3
Number of Residues	4
Details	binding site for residue CA K 501

Chain	Residue
K	MET302
K	ASP303
K	LEU307
K	SER308

site_id	AD4
Number of Residues	4
Details	binding site for residue CA K 502

Chain	Residue
K	ASP303
K	ASP309
K	TYR364
K	ASP365

site_id	AD5
Number of Residues	5
Details	binding site for residue CA K 503

Chain	Residue
K	ASP172
K	ASP178
K	ASP230
K	PHE231
K	CA504

site_id	AD6
Number of Residues	6
Details	binding site for residue CA K 504

Chain	Residue
E	GLU346
K	ASP172
K	ASP178
K	PHE231
K	ASP232
K	CA503

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	2
Details	Site: {"description":"(Microbial infection) Cleavage; by C.botulinum neurotoxin type F (BoNT/F, botF)","evidences":[{"source":"PubMed","id":"8175689","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	2
Details	Site: {"description":"(Microbial infection) Cleavage; by C.botulinum neurotoxin type D (BoNT/D, botD)","evidences":[{"source":"PubMed","id":"8175689","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	2
Details	Site: {"description":"(Microbial infection) Cleavage; by C.tetani toxin (tetX)","evidences":[{"source":"PubMed","id":"8175689","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	6
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"Q15836","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	124
Details	Domain: {"description":"t-SNARE coiled-coil homology","evidences":[{"source":"PROSITE-ProRule","id":"PRU00202","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	2
Details	Site: {"description":"(Microbial infection) Cleavage; by C.botulinum neurotoxin type C (BoNT/C)","evidences":[{"source":"PubMed","id":"7737992","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	7
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)","evidences":[{"source":"UniProtKB","id":"Q16623","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	124
Details	Domain: {"description":"t-SNARE coiled-coil homology 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00202","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	2
Details	Site: {"description":"(Microbial infection) Cleavage; by C.botulinum neurotoxin type E (BoNT/E)","evidences":[{"source":"PubMed","id":"8243676","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8294407","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8103915","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	2
Details	Site: {"description":"(Microbial infection) Cleavage; by C.botulinum neurotoxin type A (BoNT/A, botA)","evidences":[{"source":"PubMed","id":"8243676","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8294407","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8103915","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P60879","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine; by PKC","evidences":[{"source":"PubMed","id":"12459461","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	357
Details	Domain: {"description":"C2 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00041","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	266
Details	Domain: {"description":"C2 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00041","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	42
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00041","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	3
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P46096","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	3
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P46096","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	6
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"22673903","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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