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

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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

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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

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	42
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00041

Chain	Residue	Details
E	LEU171
E	ASP303
E	ASP309
E	ASP363
E	ASP365
E	ASP371
F	LEU171
F	ASP172
F	ASP178
F	ASP230
F	PHE231
E	ASP172
F	ASP232
F	SER235
F	LYS236
F	ASP238
F	ASP303
F	ASP309
F	ASP363
F	ASP365
F	ASP371
K	LEU171
E	ASP178
K	ASP172
K	ASP178
K	ASP230
K	PHE231
K	ASP232
K	SER235
K	LYS236
K	ASP238
K	ASP303
K	ASP309
E	ASP230
K	ASP363
K	ASP365
K	ASP371
E	PHE231
E	ASP232
E	SER235
E	LYS236
E	ASP238

---

site_id	SWS_FT_FI2
Number of Residues	3
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P46096

Chain	Residue	Details
E	TYR229
F	TYR229
K	TYR229
B	LYS256
H	LYS252
H	LYS253
H	LYS256

---

site_id	SWS_FT_FI3
Number of Residues	3
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P46096

Chain	Residue	Details
E	SER264
F	SER264
K	SER264

---

site_id	SWS_FT_FI4
Number of Residues	6
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903

Chain	Residue	Details
E	SER342
E	SER344
F	SER342
F	SER344
K	SER342
K	SER344

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