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3IL1

Crystal structure of the AMPA subunit GluR2 bound to the allosteric modulator, IDRA-21

Functional Information from GO Data
ChainGOidnamespacecontents
B0015276molecular_functionligand-gated monoatomic ion channel activity
B0016020cellular_componentmembrane
E0015276molecular_functionligand-gated monoatomic ion channel activity
E0016020cellular_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
BTYR220
BHOH269
BHOH287
BHOH289
BPRO89
BLEU90
BTHR91
BARG96
BGLY141
BSER142
BTHR143
BGLU193

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE GLU E 400
ChainResidue
ETYR61
EPRO89
ELEU90
ETHR91
EARG96
ELEU138
EGLY141
ESER142
ETHR143
EGLU193
ETYR220
EHOH264
EHOH267
EHOH339

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE GLU H 400
ChainResidue
HTYR61
HPRO89
HLEU90
HTHR91
HARG96
HGLY141
HSER142
HTHR143
HGLU193
HHOH270
HHOH287
HHOH296

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN B 263
ChainResidue
BGLU42
BHIS46
HGLU166

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ZN E 1
ChainResidue
EGLU42
EHIS46

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN E 262
ChainResidue
BHIS23
EASP65
EHOH743

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN H 2
ChainResidue
EHIS23
EGLU24
HHIS23
HGLU30

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN H 3
ChainResidue
BGLU166
HGLU42
HHIS46
HLEU241
HGLN244

site_idAC9
Number of Residues10
DetailsBINDING SITE FOR RESIDUE B5D B 801
ChainResidue
BLYS104
BPRO105
BVAL238
BSER242
BB5D262
EILE92
EPRO105
ESER108
ELYS218
EGLY219

site_idBC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE B5D B 262
ChainResidue
BILE92
BSER108
BSER217
BLYS218
BGLY219
BB5D801
ELYS104
EPRO105
EVAL238
ESER242
EHOH610

site_idBC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE B5D H 801
ChainResidue
HILE92
HPRO105
HPRO105
HSER108
HLYS218
HGLY219
HVAL238
HLEU239
HSER242

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues9
DetailsBINDING: BINDING => ECO:0000269|PubMed:16483599
ChainResidueDetails
BTYR61
BARG96
BGLU193
ETYR61
EARG96
EGLU193
HTYR61
HARG96
HGLU193

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING:
ChainResidueDetails
BPRO89
EPRO89
HPRO89

site_idSWS_FT_FI3
Number of Residues9
DetailsBINDING: BINDING => ECO:0000269|PubMed:25103405
ChainResidueDetails
BTHR91
BSER142
BTHR143
ETHR91
ESER142
ETHR143
HTHR91
HSER142
HTHR143

site_idSWS_FT_FI4
Number of Residues9
DetailsSITE: Interaction with the cone snail toxin Con-ikot-ikot => ECO:0000269|PubMed:25103405
ChainResidueDetails
BARG64
BARG148
BLYS240
EARG64
EARG148
ELYS240
HARG64
HARG148
HLYS240

site_idSWS_FT_FI5
Number of Residues3
DetailsSITE: Crucial to convey clamshell closure to channel opening => ECO:0000269|PubMed:25103405
ChainResidueDetails
BILE121
EILE121
HILE121

site_idSWS_FT_FI6
Number of Residues3
DetailsMOD_RES: Phosphoserine; by PKC => ECO:0000269|PubMed:8848293
ChainResidueDetails
BSER150
ESER150
HSER150

site_idSWS_FT_FI7
Number of Residues3
DetailsMOD_RES: Phosphoserine; by PKG => ECO:0000269|PubMed:8848293
ChainResidueDetails
BSER184
ESER184
HSER184

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PDB entries from 2024-05-01

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