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1PX2

Crystal Structure of Rat Synapsin I C Domain Complexed to Ca.ATP (Form 1)

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0007269biological_processneurotransmitter secretion
A0008021cellular_componentsynaptic vesicle
B0005524molecular_functionATP binding
B0007269biological_processneurotransmitter secretion
B0008021cellular_componentsynaptic vesicle
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA A 817
ChainResidue
AGLU373
AGLU386
AATP800

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA B 817
ChainResidue
BGLU373
BGLU386
BATP800
BHOH883

site_idAC3
Number of Residues16
DetailsBINDING SITE FOR RESIDUE ATP A 800
ChainResidue
AHIS274
ASER275
AGLY276
ALYS279
AGLU305
APRO306
APHE307
AILE308
ALYS336
ALEU375
AGLU386
ACA817
AHOH832
AHOH905
ALYS225
ALYS269

site_idAC4
Number of Residues24
DetailsBINDING SITE FOR RESIDUE ATP B 800
ChainResidue
BLYS225
BILE247
BVAL267
BLYS269
BALA273
BHIS274
BSER275
BGLY276
BLYS279
BGLU305
BPRO306
BPHE307
BILE308
BTRP335
BTHR337
BGLU373
BLEU375
BILE385
BGLU386
BCA817
BHOH857
BHOH863
BHOH883
BHOH916

Functional Information from PROSITE/UniProt
site_idPS00415
Number of Residues8
DetailsSYNAPSIN_1 Synapsins signature 1. LRRRLSDS
ChainResidueDetails
ALEU4-SER11

site_idPS00416
Number of Residues11
DetailsSYNAPSIN_2 Synapsins signature 2. GHAHSGMGKVK
ChainResidueDetails
AGLY271-LYS281

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"O88935","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsGlycosylation: {"description":"O-linked (GlcNAc) serine","evidences":[{"source":"PubMed","id":"12438562","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

245663

PDB entries from 2025-12-03

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