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5W5C

Crystal structure of the primed SNARE-Complexin-Synaptotagmin-1 C2AB complex

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
E0006836biological_processneurotransmitter transport
E0019905molecular_functionsyntaxin binding
F0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue MG C 101
ChainResidue
CHOH214
CHOH225
CHOH242
DHOH404
DHOH408
DHOH429

site_idAC2
Number of Residues9
Detailsbinding site for residue GOL D 301
ChainResidue
DHOH423
FLYS332
FTYR364
FHOH610
FHOH690
FHOH716
AHOH108
DSER154
DGLY155

site_idAC3
Number of Residues5
Detailsbinding site for residue GOL F 501
ChainResidue
FLYS301
FGLY306
FLEU307
FSER308
FASN333

site_idAC4
Number of Residues9
Detailsbinding site for residue GOL F 502
ChainResidue
AVAL48
AHOH104
DLEU165
FLYS325
FLYS326
FLYS327
FHOH624
FHOH664
FHOH670

site_idAC5
Number of Residues5
Detailsbinding site for residue GOL F 503
ChainResidue
FASN319
FLYS354
FTYR380
FHOH606
FHOH636

site_idAC6
Number of Residues7
Detailsbinding site for residue GOL F 504
ChainResidue
BGLU206
CARG31
CHOH206
FGLN353
FLYS354
FTYR380
FHOH617

Functional Information from PROSITE/UniProt
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 Residues14
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00041
ChainResidueDetails
FLEU171
FASP303
FASP309
FASP363
FASP365
FASP371
FASP172
FASP178
FASP230
FPHE231
FASP232
FSER235
FLYS236
FASP238

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P46096
ChainResidueDetails
FTYR229
BLYS253
BLYS256

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P46096
ChainResidueDetails
FSER264

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903
ChainResidueDetails
FSER342
FSER344

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PDB entries from 2024-07-24

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