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6FAZ

Crystal structure of the GluA2 ligand-binding domain (S1S2J) in complex with the positive allosteric modulator TDPAM01 at 1.4 A resolution.

Functional Information from GO Data
ChainGOidnamespacecontents
A0015276molecular_functionligand-gated monoatomic ion channel activity
A0016020cellular_componentmembrane
B0015276molecular_functionligand-gated monoatomic ion channel activity
B0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue SO4 A 301
ChainResidue
ASER140
ALYS144
AARG148
AHOH434
AHOH467
AHOH489
AHOH603

site_idAC2
Number of Residues4
Detailsbinding site for residue SO4 A 302
ChainResidue
AHOH420
AHOH506
ALYS82
ALYS116

site_idAC3
Number of Residues7
Detailsbinding site for residue SO4 A 303
ChainResidue
AGLU97
AASP101
APHE102
AHOH433
AHOH574
AHOH649
BLYS104

site_idAC4
Number of Residues3
Detailsbinding site for residue PEG A 304
ChainResidue
AGLY28
AARG31
ALYS52

site_idAC5
Number of Residues5
Detailsbinding site for residue PEG A 305
ChainResidue
AGLU33
ALYS253
ATRP254
ALYS258
AHOH549

site_idAC6
Number of Residues3
Detailsbinding site for residue GOL A 306
ChainResidue
AARG148
ATRP159
AARG163

site_idAC7
Number of Residues3
Detailsbinding site for residue GOL A 307
ChainResidue
AHIS46
ALYS240
AGLN244

site_idAC8
Number of Residues5
Detailsbinding site for residue GOL A 308
ChainResidue
ASER194
AGLU198
ALYS210
AASN214
AHOH595

site_idAC9
Number of Residues11
Detailsbinding site for residue GOL A 309
ChainResidue
ALEU78
AVAL79
AGLY81
ALYS117
AMET209
APRO225
ALYS226
AHOH401
AHOH403
AHOH481
AHOH632

site_idAD1
Number of Residues2
Detailsbinding site for residue CL A 310
ChainResidue
ALYS4
ATHR5

site_idAD2
Number of Residues4
Detailsbinding site for residue ACT A 311
ChainResidue
AILE152
AALA153
AHOH439
AHOH619

site_idAD3
Number of Residues13
Detailsbinding site for residue GLU A 312
ChainResidue
ATYR61
APRO89
ALEU90
ATHR91
AARG96
AGLY141
ASER142
ATHR143
AGLU193
ATYR220
AHOH432
AHOH468
AHOH488

site_idAD4
Number of Residues4
Detailsbinding site for residue EDO A 313
ChainResidue
AASN214
AASP216
ASER217
BASP248

site_idAD5
Number of Residues14
Detailsbinding site for residue D45 B 301
ChainResidue
ALYS104
APRO105
ASER108
ASER217
ALYS218
AGLY219
AASN242
BLYS104
BPRO105
BSER108
BLYS218
BGLY219
BASN242
BHOH524

site_idAD6
Number of Residues7
Detailsbinding site for residue SO4 B 302
ChainResidue
BSER140
BLYS144
BARG148
BHOH423
BHOH435
BHOH547
BHOH570

site_idAD7
Number of Residues5
Detailsbinding site for residue SO4 B 303
ChainResidue
BARG31
BHOH425
BHOH460
BHOH482
BHOH494

site_idAD8
Number of Residues4
Detailsbinding site for residue GOL B 304
ChainResidue
BARG163
BHOH598
BARG148
BTRP159

site_idAD9
Number of Residues2
Detailsbinding site for residue CL B 305
ChainResidue
BASN22
BGLU24

site_idAE1
Number of Residues2
Detailsbinding site for residue CL B 306
ChainResidue
BHIS46
BGLN244

site_idAE2
Number of Residues3
Detailsbinding site for residue CL B 307
ChainResidue
BLYS50
BTYR51
BHOH589

site_idAE3
Number of Residues1
Detailsbinding site for residue CL B 308
ChainResidue
BALA153

site_idAE4
Number of Residues6
Detailsbinding site for residue ACT B 309
ChainResidue
AASP248
BASN214
BLEU215
BASP216
BSER217
BHOH587

site_idAE5
Number of Residues6
Detailsbinding site for residue ACT B 310
ChainResidue
ALYS104
AHOH694
BGLU97
BASP101
BPHE102
BHOH610

site_idAE6
Number of Residues13
Detailsbinding site for residue GLU B 311
ChainResidue
BTYR61
BPRO89
BLEU90
BTHR91
BARG96
BGLY141
BSER142
BTHR143
BGLU193
BTYR220
BHOH444
BHOH462
BHOH463

site_idAE7
Number of Residues7
Detailsbinding site for residue EDO B 312
ChainResidue
BALA134
BTYR161
BALA165
BGLU166
BPRO167
BVAL169
BARG180

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:11086992, ECO:0000269|PubMed:16483599, ECO:0007744|PDB:1FTJ, ECO:0007744|PDB:2CMO
ChainResidueDetails
APRO89
BSER142
BTHR143
BGLU193
ATHR91
AARG96
ASER142
ATHR143
AGLU193
BPRO89
BTHR91
BARG96

site_idSWS_FT_FI2
Number of Residues6
DetailsSITE: Interaction with the cone snail toxin Con-ikot-ikot => ECO:0000269|PubMed:25103405
ChainResidueDetails
AARG64
AARG148
ALYS240
BARG64
BARG148
BLYS240

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Crucial to convey clamshell closure to channel opening => ECO:0000269|PubMed:25103405
ChainResidueDetails
AILE121
BILE121

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PKC => ECO:0000269|PubMed:8848293
ChainResidueDetails
ASER150
BSER150

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PKG => ECO:0000269|PubMed:8848293
ChainResidueDetails
ASER184
BSER184

site_idSWS_FT_FI6
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN3
BASN3

222624

PDB entries from 2024-07-17

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