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6EPA

Structure of dNCS-1 bound to the NCS-1/Ric8a protein/protein interaction regulator IGS-1.76

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 201
ChainResidue
AASP73
AASN75
AASP77
AALA79
AGLU84
AHOH331

site_idAC2
Number of Residues6
Detailsbinding site for residue CA A 202
ChainResidue
AARG162
AGLU167
AHOH304
AASP156
AASN158
AASP160

site_idAC3
Number of Residues6
Detailsbinding site for residue CA A 203
ChainResidue
AASP109
AASP111
AASP113
ATYR115
AGLU120
AHOH351

site_idAC4
Number of Residues7
Detailsbinding site for residue BNQ A 204
ChainResidue
ATRP30
AILE51
ATYR52
ATHR92
ATRP103
ALEU182
AHOH349

site_idAC5
Number of Residues5
Detailsbinding site for residue NA A 206
ChainResidue
AARG70
AASP73
AASN76
AHOH311
AHOH405

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

222415

PDB entries from 2024-07-10

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