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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

6MTI

Synaptotagmin-1 C2A, C2B domains and SNARE-pin proteins (5CCI) individually docked into Cryo-EM map of C2AB-SNARE complexes helically organized on lipid nanotube surface in presence of Mg2+

Functional Information from GO Data
ChainGOidnamespacecontents
10016020cellular_componentmembrane
20016020cellular_componentmembrane
30016020cellular_componentmembrane
40016020cellular_componentmembrane
50016020cellular_componentmembrane
60016020cellular_componentmembrane
A0016020cellular_componentmembrane
A0016192biological_processvesicle-mediated transport
B0005484molecular_functionSNAP receptor activity
B0006886biological_processintracellular protein transport
B0016020cellular_componentmembrane
B0016192biological_processvesicle-mediated transport
C0000149molecular_functionSNARE binding
C0005249molecular_functionvoltage-gated potassium channel activity
C0017075molecular_functionsyntaxin-1 binding
E0016020cellular_componentmembrane
E0016192biological_processvesicle-mediated transport
F0005484molecular_functionSNAP receptor activity
F0006886biological_processintracellular protein transport
F0016020cellular_componentmembrane
F0016192biological_processvesicle-mediated transport
G0000149molecular_functionSNARE binding
G0005249molecular_functionvoltage-gated potassium channel activity
G0017075molecular_functionsyntaxin-1 binding
I0016020cellular_componentmembrane
I0016192biological_processvesicle-mediated transport
J0005484molecular_functionSNAP receptor activity
J0006886biological_processintracellular protein transport
J0016020cellular_componentmembrane
J0016192biological_processvesicle-mediated transport
K0000149molecular_functionSNARE binding
K0005249molecular_functionvoltage-gated potassium channel activity
K0017075molecular_functionsyntaxin-1 binding
M0016020cellular_componentmembrane
M0016192biological_processvesicle-mediated transport
N0005484molecular_functionSNAP receptor activity
N0006886biological_processintracellular protein transport
N0016020cellular_componentmembrane
N0016192biological_processvesicle-mediated transport
O0000149molecular_functionSNARE binding
O0005249molecular_functionvoltage-gated potassium channel activity
O0017075molecular_functionsyntaxin-1 binding
Q0016020cellular_componentmembrane
Q0016192biological_processvesicle-mediated transport
R0005484molecular_functionSNAP receptor activity
R0006886biological_processintracellular protein transport
R0016020cellular_componentmembrane
R0016192biological_processvesicle-mediated transport
S0000149molecular_functionSNARE binding
S0005249molecular_functionvoltage-gated potassium channel activity
S0017075molecular_functionsyntaxin-1 binding
U0016020cellular_componentmembrane
U0016192biological_processvesicle-mediated transport
V0005484molecular_functionSNAP receptor activity
V0006886biological_processintracellular protein transport
V0016020cellular_componentmembrane
V0016192biological_processvesicle-mediated transport
W0000149molecular_functionSNARE binding
W0005249molecular_functionvoltage-gated potassium channel activity
W0017075molecular_functionsyntaxin-1 binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue MG 1 301
ChainResidue
1ASP172
1ASP178
1PHE231
1ASP232
site_idAC2
Number of Residues4
Detailsbinding site for residue MG 2 801
ChainResidue
2ASP172
2ASP178
2PHE231
2ASP232
site_idAC3
Number of Residues5
Detailsbinding site for residue MG 2 802
ChainResidue
2ASP590
2ASP644
2TYR645
2ASP646
2ASP584
site_idAC4
Number of Residues4
Detailsbinding site for residue MG 3 801
ChainResidue
3ASP172
3ASP178
3PHE231
3ASP232
site_idAC5
Number of Residues5
Detailsbinding site for residue MG 3 802
ChainResidue
3ASP584
3ASP590
3ASP644
3TYR645
3ASP646
site_idAC6
Number of Residues4
Detailsbinding site for residue MG 4 801
ChainResidue
4ASP172
4ASP178
4PHE231
4ASP232
site_idAC7
Number of Residues5
Detailsbinding site for residue MG 4 802
ChainResidue
4ASP584
4ASP590
4ASP644
4TYR645
4ASP646
site_idAC8
Number of Residues4
Detailsbinding site for residue MG 5 801
ChainResidue
5ASP172
5ASP178
5PHE231
5ASP232
site_idAC9
Number of Residues5
Detailsbinding site for residue MG 5 802
ChainResidue
5ASP584
5ASP590
5ASP644
5TYR645
5ASP646
site_idAD1
Number of Residues4
Detailsbinding site for residue MG 6 301
ChainResidue
6ASP172
6ASP178
6PHE231
6ASP232
Functional Information from PROSITE/UniProt
site_idPS00417
Number of Residues20
DetailsSYNAPTOBREVIN Synaptobrevin signature. NVDKVlERdqKLSeLdDRAD
ChainResidueDetails
UASN49-ASP68
site_idPS00914
Number of Residues40
DetailsSYNTAXIN Syntaxin / epimorphin family signature. RhseIikLEnsIrELhdMFmdMamlVesQGemIDrIEyn.V
ChainResidueDetails
VARG198-VAL237
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues714
DetailsDomain: {"description":"C2 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00041","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues74
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00041","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues6
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P46096","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues6
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P46096","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues532
DetailsDomain: {"description":"C2 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00041","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues8
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"22673903","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues6
DetailsSite: {"description":"(Microbial infection) Cleavage; by C.botulinum neurotoxin type F (BoNT/F, botF)","evidences":[{"source":"PubMed","id":"8505288","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues6
DetailsSite: {"description":"(Microbial infection) Cleavage; by C.botulinum neurotoxin type D (BoNT/D, botD)","evidences":[{"source":"PubMed","id":"8175689","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues6
DetailsSite: {"description":"(Microbial infection) Cleavage; by C.botulinum neurotoxin type X (BoNT/X)","evidences":[{"source":"PubMed","id":"28770820","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues6
DetailsSite: {"description":"(Microbial infection) Cleavage; by C.tetani tetanus toxin (tetX)","evidences":[{"source":"PubMed","id":"1331807","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues6
DetailsSite: {"description":"(Microbial infection) Cleavage; by C.botulinum neurotoxin type G (BoNT/G, botG)","evidences":[{"source":"PubMed","id":"7910017","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues372
DetailsDomain: {"description":"t-SNARE coiled-coil homology","evidences":[{"source":"PROSITE-ProRule","id":"PRU00202","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues6
DetailsSite: {"description":"(Microbial infection) Cleavage; by C.botulinum neurotoxin type C (BoNT/C)","evidences":[{"source":"PubMed","id":"7737992","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues24
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)","evidences":[{"source":"UniProtKB","id":"Q16623","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues372
DetailsDomain: {"description":"t-SNARE coiled-coil homology 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00202","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues6
DetailsSite: {"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"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues6
DetailsSite: {"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"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues6
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P60879","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues6
DetailsModified residue: {"description":"Phosphoserine; by PKC","evidences":[{"source":"PubMed","id":"12459461","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

248335

PDB entries from 2026-01-28

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