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8JLF

Cryo-EM structure of SV2A in complex with BoNT/A2 Hc

Functional Information from PROSITE/UniProt
site_idPS00217
Number of Residues26
DetailsSUGAR_TRANSPORT_2 Sugar transport proteins signature 2. LsGVGiGGsipivfsYfsEflaqekR
ChainResidueDetails
ALEU264-ARG289

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues240
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
APHE170-LEU190
AMET206-ALA226
ACYS234-GLY254
ALEU263-PHE283
ATRP295-ILE315
AVAL335-PRO355
ALEU448-PHE468
APHE599-MET619
AMET627-SER647
AILE652-LEU672
APHE686-VAL708
AALA713-LEU731

site_idSWS_FT_FI2
Number of Residues174
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
APRO191-GLY205
ATYR255-ARG262
APRO316-ARG334
APRO469-TYR598
AGLU648-MET651
AGLY709-LYS712

site_idSWS_FT_FI3
Number of Residues135
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
AASP227-GLN233
ALEU284-SER294
AGLU356-THR447
AASP620-ARG626
ATHR673-ALA685
ALYS732-GLN742

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332
ChainResidueDetails
ASER80
ASER81

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19690332
ChainResidueDetails
ATHR84

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9JIS5
ChainResidueDetails
ASER127

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q02563
ChainResidueDetails
ASER393

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q9JIS5
ChainResidueDetails
ATYR480

site_idSWS_FT_FI9
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN498
AASN548
AASN573

220472

PDB entries from 2024-05-29

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