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4FAT

Ligand-binding domain of GluA2 (flip) ionotropic glutamate receptor in complex with an allosteric modulator

Functional Information from GO Data
ChainGOidnamespacecontents
A0015276molecular_functionligand-gated monoatomic ion channel activity
A0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE GLU A 301
ChainResidue
ATYR61
AHOH422
AHOH426
AHOH430
APRO89
ALEU90
ATHR91
AARG96
AGLY141
ASER142
ATHR143
AGLU193

site_idAC2
Number of Residues21
DetailsBINDING SITE FOR RESIDUE 496 A 302
ChainResidue
AILE92
APRO105
APRO105
APHE106
APHE106
AMET107
ASER108
ASER108
ASER217
ASER217
ALYS218
ALYS218
AGLY219
AGLY219
ALEU239
ALEU239
ASER242
ASER242
AHOH460
AHOH649
AHOH650

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 303
ChainResidue
AHIS23
AGLU24
AARG31
AHIS46
ALYS240
AHOH723
AHOH732
AHOH770
AHOH771

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 304
ChainResidue
AGLU27
AGLY28
AASN29
AGLU30
AARG149
ALYS151
AHOH551
AHOH604

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 305
ChainResidue
AASP139
ASER140
ALYS144
AGLU145
AARG148
AGOL306
AHOH503
AHOH543
AHOH685

site_idAC6
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL A 306
ChainResidue
AGLY62
AALA63
ATRP71
ATHR93
AVAL95
AARG96
AGLY141
AGLU145
ASO4305
AHOH419
AHOH658

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 307
ChainResidue
AARG148
ATRP159
AARG163
AHOH741

site_idAC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 308
ChainResidue
ASER108
ALEU109
ASER194
ATHR195
AGLU198
AASN214
AHOH471
AHOH605
AHOH774

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 309
ChainResidue
AASN214
AASP216
ASER217
AASP248
AHOH638
AHOH715

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE LI A 310
ChainResidue
AGLU97
AILE100
AASP101
AHOH427

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11086992","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16483599","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1FTJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CMO","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsSite: {"description":"Interaction with the cone snail toxin Con-ikot-ikot","evidences":[{"source":"PubMed","id":"25103405","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsSite: {"description":"Crucial to convey clamshell closure to channel opening","evidences":[{"source":"PubMed","id":"25103405","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by PKC","evidences":[{"source":"PubMed","id":"8848293","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by PKG","evidences":[{"source":"PubMed","id":"8848293","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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