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3IJX

Crystal structure of the AMPA subunit GluR2 bound to the allosteric modulator, hydrochlorothiazide

Functional Information from GO Data
ChainGOidnamespacecontents
B0015276molecular_functionligand-gated monoatomic ion channel activity
B0016020cellular_componentmembrane
D0015276molecular_functionligand-gated monoatomic ion channel activity
D0016020cellular_componentmembrane
H0015276molecular_functionligand-gated monoatomic ion channel activity
H0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE GLU B 400
ChainResidue
BTYR61
BGLU193
BHOH263
BHOH266
BHOH302
BPRO89
BLEU90
BTHR91
BARG96
BLEU138
BGLY141
BSER142
BTHR143

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GLU D 400
ChainResidue
DTYR61
DPRO89
DLEU90
DTHR91
DARG96
DLEU138
DGLY141
DSER142
DTHR143
DGLU193
DHOH266

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GLU H 400
ChainResidue
HTYR61
HPRO89
HLEU90
HTHR91
HARG96
HLEU138
HGLY141
HSER142
HTHR143
HGLU193

site_idAC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE HCZ B 800
ChainResidue
BLYS104
BPRO105
BSER108
BLEU239
BSER242
DILE92
DSER108
DSER217
DLYS218
DGLY219
DHCZ800

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE HCZ D 800
ChainResidue
BILE92
BSER108
BSER217
BLYS218
BHCZ800
DLYS104
DPRO105
DSER108
DLEU239
DSER242

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE HCZ H 800
ChainResidue
HILE92
HLYS104
HPRO105
HSER108
HSER108
HSER217
HLYS218
HLEU239
HSER242
HHOH313

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ZN D 1
ChainResidue
DGLU42
DHIS46

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ZN H 2
ChainResidue
HZN3
HGLU166

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN H 3
ChainResidue
BGLU42
BHIS46
HZN2
HGLU166

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN B 262
ChainResidue
BHIS23
DASP65
DASP67

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN H 262
ChainResidue
HGLU42
HHIS46
HLEU241

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues18
DetailsBINDING: BINDING => ECO:0000269|PubMed:11086992, ECO:0000269|PubMed:16483599, ECO:0007744|PDB:1FTJ, ECO:0007744|PDB:2CMO
ChainResidueDetails
BPRO89
DSER142
DTHR143
DGLU193
HPRO89
HTHR91
HARG96
HSER142
HTHR143
HGLU193
BTHR91
BARG96
BSER142
BTHR143
BGLU193
DPRO89
DTHR91
DARG96

site_idSWS_FT_FI2
Number of Residues9
DetailsSITE: Interaction with the cone snail toxin Con-ikot-ikot => ECO:0000269|PubMed:25103405
ChainResidueDetails
BARG64
BARG148
BLYS240
DARG64
DARG148
DLYS240
HARG64
HARG148
HLYS240

site_idSWS_FT_FI3
Number of Residues3
DetailsSITE: Crucial to convey clamshell closure to channel opening => ECO:0000269|PubMed:25103405
ChainResidueDetails
BILE121
DILE121
HILE121

site_idSWS_FT_FI4
Number of Residues3
DetailsMOD_RES: Phosphoserine; by PKC => ECO:0000269|PubMed:8848293
ChainResidueDetails
BSER150
DSER150
HSER150

site_idSWS_FT_FI5
Number of Residues3
DetailsMOD_RES: Phosphoserine; by PKG => ECO:0000269|PubMed:8848293
ChainResidueDetails
BSER184
DSER184
HSER184

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PDB entries from 2024-08-07

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