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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
DetailsMOD_RES: Phosphoserine; by CaMK1 and PKA => ECO:0000305|PubMed:10571231
ChainResidueDetails
ASER9
BSER9

site_idSWS_FT_FI2
Number of Residues6
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903
ChainResidueDetails
ASER39
ASER62
ASER67
BSER39
BSER62
BSER67

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:O88935
ChainResidueDetails
ATYR312
BTYR312

site_idSWS_FT_FI4
Number of Residues2
DetailsCARBOHYD: O-linked (GlcNAc) serine => ECO:0000269|PubMed:10386995, ECO:0000269|PubMed:12438562
ChainResidueDetails
ASER55
BSER55

site_idSWS_FT_FI5
Number of Residues2
DetailsCARBOHYD: O-linked (GlcNAc) threonine => ECO:0000305|PubMed:10386995
ChainResidueDetails
ATHR56
BTHR56

site_idSWS_FT_FI6
Number of Residues2
DetailsCARBOHYD: O-linked (GlcNAc) threonine => ECO:0000269|PubMed:10386995, ECO:0000269|PubMed:12438562
ChainResidueDetails
ATHR87
BTHR87

site_idSWS_FT_FI7
Number of Residues4
DetailsCARBOHYD: O-linked (GlcNAc) serine => ECO:0000269|PubMed:12438562
ChainResidueDetails
ASER96
ASER261
BSER96
BSER261

site_idSWS_FT_FI8
Number of Residues2
DetailsCARBOHYD: O-linked (GlcNAc) serine => ECO:0000305|PubMed:12438562
ChainResidueDetails
ASER103
BSER103

222926

PDB entries from 2024-07-24

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