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1PK8

Crystal Structure of Rat Synapsin I C Domain Complexed to Ca.ATP

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0007269biological_processneurotransmitter secretion
A0008021cellular_componentsynaptic vesicle
B0005524molecular_functionATP binding
B0007269biological_processneurotransmitter secretion
B0008021cellular_componentsynaptic vesicle
C0005524molecular_functionATP binding
C0007269biological_processneurotransmitter secretion
C0008021cellular_componentsynaptic vesicle
D0005524molecular_functionATP binding
D0007269biological_processneurotransmitter secretion
D0008021cellular_componentsynaptic vesicle
E0005524molecular_functionATP binding
E0007269biological_processneurotransmitter secretion
E0008021cellular_componentsynaptic vesicle
F0005524molecular_functionATP binding
F0007269biological_processneurotransmitter secretion
F0008021cellular_componentsynaptic vesicle
G0005524molecular_functionATP binding
G0007269biological_processneurotransmitter secretion
G0008021cellular_componentsynaptic vesicle
H0005524molecular_functionATP binding
H0007269biological_processneurotransmitter secretion
H0008021cellular_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 Residues3
DetailsBINDING SITE FOR RESIDUE CA B 817
ChainResidue
BGLU373
BGLU386
BATP801

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA C 817
ChainResidue
CGLU373
CGLU386
CATP802

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA D 817
ChainResidue
DGLU373
DGLU386
DATP803

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA E 817
ChainResidue
EGLU373
EGLU386
EATP804

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA F 817
ChainResidue
FGLU373
FGLU386
FATP805

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA G 817
ChainResidue
GGLU373
GGLU386
GATP806

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA H 817
ChainResidue
HGLU373
HGLU386
HATP807
HHOH842

site_idAC9
Number of Residues26
DetailsBINDING SITE FOR RESIDUE ATP A 800
ChainResidue
ALYS225
AVAL267
ALYS269
AHIS274
ASER275
AGLY276
ALYS279
AGLU305
APRO306
AILE308
AASP313
AARG328
ATRP335
ALYS336
ATHR337
AASN338
AGLU373
ALEU375
AGLU386
AVAL388
ACA817
AHOH831
AHOH859
AHOH903
AHOH916
AHOH935

site_idBC1
Number of Residues26
DetailsBINDING SITE FOR RESIDUE ATP B 801
ChainResidue
BLYS225
BVAL267
BLYS269
BHIS274
BSER275
BGLY276
BLYS279
BGLU305
BPRO306
BPHE307
BILE308
BASP313
BARG328
BTRP335
BLYS336
BTHR337
BASN338
BGLU373
BLEU375
BILE385
BGLU386
BVAL388
BCA817
BHOH842
BHOH890
BHOH900

site_idBC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE ATP C 802
ChainResidue
CLYS225
CILE247
CVAL267
CLYS269
CHIS274
CSER275
CGLY276
CLYS279
CGLU305
CPRO306
CPHE307
CILE308
CARG328
CTRP335
CGLU373
CLEU375
CGLU386
CCA817

site_idBC3
Number of Residues26
DetailsBINDING SITE FOR RESIDUE ATP D 803
ChainResidue
DHIS274
DSER275
DGLY276
DLYS279
DGLU305
DPRO306
DPHE307
DILE308
DASP313
DARG328
DTRP335
DLYS336
DTHR337
DASN338
DGLU373
DLEU375
DILE385
DGLU386
DCA817
DHOH869
DHOH874
DHOH892
DLYS225
DILE247
DVAL267
DLYS269

site_idBC4
Number of Residues21
DetailsBINDING SITE FOR RESIDUE ATP E 804
ChainResidue
ELYS225
EILE247
EVAL267
ELYS269
EHIS274
ESER275
EGLY276
ELYS279
EGLU305
EPRO306
EPHE307
EILE308
EARG328
ETRP335
ELYS336
ETHR337
EGLU373
ELEU375
EGLU386
ECA817
EHOH870

site_idBC5
Number of Residues24
DetailsBINDING SITE FOR RESIDUE ATP F 805
ChainResidue
FLYS225
FILE247
FVAL267
FLYS269
FALA273
FHIS274
FSER275
FGLY276
FLYS279
FGLU305
FPRO306
FPHE307
FILE308
FASP313
FARG328
FTRP335
FLYS336
FTHR337
FGLU373
FLEU375
FGLU386
FVAL388
FCA817
FHOH848

site_idBC6
Number of Residues24
DetailsBINDING SITE FOR RESIDUE ATP G 806
ChainResidue
GLYS225
GILE247
GVAL267
GLYS269
GHIS274
GSER275
GGLY276
GLYS279
GGLU305
GPRO306
GPHE307
GILE308
GASP313
GARG328
GTRP335
GLYS336
GTHR337
GASN338
GGLU373
GLEU375
GGLU386
GCA817
GHOH880
GHOH885

site_idBC7
Number of Residues21
DetailsBINDING SITE FOR RESIDUE ATP H 807
ChainResidue
HLYS225
HILE247
HVAL267
HLYS269
HHIS274
HSER275
HGLY276
HLYS279
HGLU305
HPRO306
HPHE307
HILE308
HARG328
HTRP335
HGLU373
HLEU375
HGLU386
HVAL388
HCA817
HHOH842
HHOH855

site_idBC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 818
ChainResidue
AHIS217
APHE364
AHOH879
AHOH902
BHIS217
BPHE364

site_idBC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 819
ChainResidue
BASP120
BTHR124
BTRP126
BARG186
BHOH896

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 Residues8
DetailsMOD_RES: Phosphoserine; by CaMK1 and PKA => ECO:0000305|PubMed:10571231
ChainResidueDetails
ASER9
BSER9
CSER9
DSER9
ESER9
FSER9
GSER9
HSER9

site_idSWS_FT_FI2
Number of Residues24
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903
ChainResidueDetails
ASER39
DSER39
DSER62
DSER67
ESER39
ESER62
ESER67
FSER39
FSER62
FSER67
GSER39
ASER62
GSER62
GSER67
HSER39
HSER62
HSER67
ASER67
BSER39
BSER62
BSER67
CSER39
CSER62
CSER67

site_idSWS_FT_FI3
Number of Residues8
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:O88935
ChainResidueDetails
ATYR312
BTYR312
CTYR312
DTYR312
ETYR312
FTYR312
GTYR312
HTYR312

site_idSWS_FT_FI4
Number of Residues8
DetailsCARBOHYD: O-linked (GlcNAc) serine => ECO:0000269|PubMed:10386995, ECO:0000269|PubMed:12438562
ChainResidueDetails
ASER55
BSER55
CSER55
DSER55
ESER55
FSER55
GSER55
HSER55

site_idSWS_FT_FI5
Number of Residues8
DetailsCARBOHYD: O-linked (GlcNAc) threonine => ECO:0000305|PubMed:10386995
ChainResidueDetails
ATHR56
BTHR56
CTHR56
DTHR56
ETHR56
FTHR56
GTHR56
HTHR56

site_idSWS_FT_FI6
Number of Residues8
DetailsCARBOHYD: O-linked (GlcNAc) threonine => ECO:0000269|PubMed:10386995, ECO:0000269|PubMed:12438562
ChainResidueDetails
ATHR87
BTHR87
CTHR87
DTHR87
ETHR87
FTHR87
GTHR87
HTHR87

site_idSWS_FT_FI7
Number of Residues16
DetailsCARBOHYD: O-linked (GlcNAc) serine => ECO:0000269|PubMed:12438562
ChainResidueDetails
ASER96
ESER261
FSER96
FSER261
GSER96
GSER261
HSER96
HSER261
ASER261
BSER96
BSER261
CSER96
CSER261
DSER96
DSER261
ESER96

site_idSWS_FT_FI8
Number of Residues8
DetailsCARBOHYD: O-linked (GlcNAc) serine => ECO:0000305|PubMed:12438562
ChainResidueDetails
ASER103
BSER103
CSER103
DSER103
ESER103
FSER103
GSER103
HSER103

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PDB entries from 2024-11-06

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