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5G08

Crystal structure of Drosophila NCS-1 bound to chlorpromazine

Functional Information from GO Data
ChainGOidnamespacecontents
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0007268biological_processchemical synaptic transmission
A0007269biological_processneurotransmitter secretion
A0007528biological_processneuromuscular junction development
A0008021cellular_componentsynaptic vesicle
A0008048molecular_functioncalcium sensitive guanylate cyclase activator activity
A0016192biological_processvesicle-mediated transport
A0046872molecular_functionmetal ion binding
A0046928biological_processregulation of neurotransmitter secretion
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1184
ChainResidue
AASP73
AASN75
AASP77
AALA79
AGLU84
AHOH2090

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1185
ChainResidue
AARG162
AGLU167
AHOH2139
AASP156
AASN158
AASP160

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1186
ChainResidue
AASP109
AASP111
AASP113
ATYR115
AGLU120
AHOH2114

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE Z80 A 1187
ChainResidue
ATYR52
APHE72
APHE85
ATHR92
AGOL1188
AEDO1190
AHOH2045

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 1188
ChainResidue
ATRP30
APHE85
AZ801187
AEDO1190

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 1189
ChainResidue
ATHR18
AASP19
ATHR20
AHOH2160
AHOH2161

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 1190
ChainResidue
AASP37
AILE51
AZ801187
AGOL1188
AHOH2164

Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DENNDGAIEfeEF
ChainResidueDetails
AASP73-PHE85
AASP109-MET121
AASP156-PHE168

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues15
DetailsBINDING: BINDING => ECO:0000269|PubMed:25074811, ECO:0000269|PubMed:28119500, ECO:0000269|PubMed:29966094, ECO:0007744|PDB:4BY4, ECO:0007744|PDB:4BY5, ECO:0007744|PDB:5AAN, ECO:0007744|PDB:5FYX, ECO:0007744|PDB:5G08, ECO:0007744|PDB:6EPA
ChainResidueDetails
AASP73
AGLU120
AASP156
AASN158
AASP160
AARG162
AGLU167
AASN75
AASP77
AALA79
AGLU84
AASP109
AASP111
AASP113
ATYR115

site_idSWS_FT_FI2
Number of Residues1
DetailsLIPID: N-myristoyl glycine => ECO:0000250|UniProtKB:P62168
ChainResidueDetails
AGLY2

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PDB entries from 2024-07-10

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