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5CCH

Structure of the Ca2+-bound synaptotagmin-1 SNARE complex (short unit cell form)

Functional Information from GO Data
ChainGOidnamespacecontents
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
F0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue CA E 501
ChainResidue
EASP303
ESER308
EASP309
EASP363
ETYR364
EASP365
ECA502

site_idAC2
Number of Residues4
Detailsbinding site for residue CA E 502
ChainResidue
EASP365
ECA501
EMET302
EASP363

site_idAC3
Number of Residues4
Detailsbinding site for residue CA E 503
ChainResidue
EASP172
EASP178
EPHE231
EASP232

site_idAC4
Number of Residues6
Detailsbinding site for residue CA F 501
ChainResidue
FASP172
FASP230
FPHE231
FASP232
FLYS324
FCA502

site_idAC5
Number of Residues6
Detailsbinding site for residue CA F 502
ChainResidue
FASP172
FASP178
FASP230
FPHE231
FASP232
FCA501

site_idAC6
Number of Residues3
Detailsbinding site for residue CA F 503
ChainResidue
FASP309
FTYR364
FCA504

site_idAC7
Number of Residues4
Detailsbinding site for residue CA F 504
ChainResidue
FASP363
FTYR364
FASP365
FCA503

Functional Information from PROSITE/UniProt
site_idPS00417
Number of Residues20
DetailsSYNAPTOBREVIN Synaptobrevin signature. NVDKVlERdqKLSeLdDRAD
ChainResidueDetails
AASN49-ASP68

site_idPS00914
Number of Residues40
DetailsSYNTAXIN Syntaxin / epimorphin family signature. RhseIikLEnsIrELhdMFmdMamlVesQGemIDrIEyn.V
ChainResidueDetails
BARG198-VAL237

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues28
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00041
ChainResidueDetails
ELEU171
EASP303
EASP309
EASP363
EASP365
EASP371
FLEU171
FASP172
FASP178
FASP230
FPHE231
EASP172
FASP232
FSER235
FLYS236
FASP238
FASP303
FASP309
FASP363
FASP365
FASP371
EASP178
EASP230
EPHE231
EASP232
ESER235
ELYS236
EASP238

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P46096
ChainResidueDetails
ETYR229
FTYR229
BLYS253
BLYS256

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P46096
ChainResidueDetails
ESER264
FSER264

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903
ChainResidueDetails
ESER342
ESER344
FSER342
FSER344

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: (Microbial infection) Cleavage; by C.botulinum neurotoxin type G (BoNT/G, botG) => ECO:0000269|PubMed:7910017
ChainResidueDetails
AALA81

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PDB entries from 2024-07-24

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