Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4BY5

Crystal structure of Drosophila Frq2

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
B0005509molecular_functioncalcium ion binding
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0007268biological_processchemical synaptic transmission
B0007269biological_processneurotransmitter secretion
B0007528biological_processneuromuscular junction development
B0008021cellular_componentsynaptic vesicle
B0008048molecular_functioncalcium sensitive guanylate cyclase activator activity
B0016192biological_processvesicle-mediated transport
B0046872molecular_functionmetal ion binding
B0046928biological_processregulation of neurotransmitter secretion
C0005509molecular_functioncalcium ion binding
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0007268biological_processchemical synaptic transmission
C0007269biological_processneurotransmitter secretion
C0007528biological_processneuromuscular junction development
C0008021cellular_componentsynaptic vesicle
C0008048molecular_functioncalcium sensitive guanylate cyclase activator activity
C0016192biological_processvesicle-mediated transport
C0046872molecular_functionmetal ion binding
C0046928biological_processregulation of neurotransmitter secretion
D0005509molecular_functioncalcium ion binding
D0005515molecular_functionprotein binding
D0005737cellular_componentcytoplasm
D0007268biological_processchemical synaptic transmission
D0007269biological_processneurotransmitter secretion
D0007528biological_processneuromuscular junction development
D0008021cellular_componentsynaptic vesicle
D0008048molecular_functioncalcium sensitive guanylate cyclase activator activity
D0016192biological_processvesicle-mediated transport
D0046872molecular_functionmetal ion binding
D0046928biological_processregulation of neurotransmitter secretion
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1183
ChainResidue
AASP73
AASN75
AASP77
AALA79
AGLU84
AHOH2069

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1184
ChainResidue
ATYR115
AGLU120
AHOH2081
AASP109
AASP111
AASP113

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1185
ChainResidue
AASP156
AASN158
AASP160
AARG162
AGLU167
AHOH2093

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 1185
ChainResidue
BASP73
BASN75
BASP77
BALA79
BGLU84
BHOH2029

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 1186
ChainResidue
BASP156
BASN158
BASP160
BARG162
BGLU167
BHOH2055

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA C 1185
ChainResidue
CASP73
CASN75
CASP77
CALA79
CGLU84
CHOH2020

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA C 1186
ChainResidue
CASP109
CASP111
CASP113
CTYR115
CGLU120
CHOH2033

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA C 1187
ChainResidue
CASP156
CASN158
CASP160
CARG162
CGLU167
CHOH2036

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA D 1183
ChainResidue
DASP73
DASN75
DASP77
DALA79
DGLU84
DHOH2005

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA D 1184
ChainResidue
DASP156
DASN158
DASP160
DARG162
DGLU167
DHOH2017

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA D 1185
ChainResidue
DASP109
DASP111
DASP113
DTYR115
DGLU120

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 1187
ChainResidue
BASP109
BASP111
BASP113
BTYR115
BGLU120
BHOH2043

site_idBC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA B 1188
ChainResidue
BARG70
BASP73
BASN76
BHOH2021
BHOH2022
BHOH2026

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 Residues60
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
BASP73
BASN75
BASP77
BALA79
AASN75
BGLU84
BASP109
BASP111
BASP113
BTYR115
BGLU120
BASP156
BASN158
BASP160
BARG162
AASP77
BGLU167
CASP73
CASN75
CASP77
CALA79
CGLU84
CASP109
CASP111
CASP113
CTYR115
AALA79
CGLU120
CASP156
CASN158
CASP160
CARG162
CGLU167
DASP73
DASN75
DASP77
DALA79
AGLU84
DGLU84
DASP109
DASP111
DASP113
DTYR115
DGLU120
DASP156
DASN158
DASP160
DARG162
AASP109
DGLU167
AASP111
AASP113
ATYR115

site_idSWS_FT_FI2
Number of Residues4
DetailsLIPID: N-myristoyl glycine => ECO:0000250|UniProtKB:P62168
ChainResidueDetails
AGLY2
BGLY2
CGLY2
DGLY2

222415

PDB entries from 2024-07-10

PDB statisticsPDBj update infoContact PDBjnumon