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5NS9

Crystal structure of the GluA2 LBD (L483Y-N754S-L758V) in complex with glutamate

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 Residues12
Detailsbinding site for residue 1PE A 301
ChainResidue
ALYS117
AHOH484
AHOH529
AHOH769
AGLU201
AGLN202
ALYS226
ASER228
ACYS261
AGLY262
ASER263
A1PE302

site_idAC2
Number of Residues11
Detailsbinding site for residue 1PE A 302
ChainResidue
AVAL6
APHE49
ASER228
ASER229
ACYS261
AGLY262
ASER263
A1PE301
AHOH412
AHOH514
AHOH595

site_idAC3
Number of Residues7
Detailsbinding site for residue PG0 A 303
ChainResidue
ALYS4
AVAL7
ALYS82
AASP84
APRO205
AHOH493
AHOH645

site_idAC4
Number of Residues3
Detailsbinding site for residue SO4 A 304
ChainResidue
AARG149
AHOH432
AHOH482

site_idAC5
Number of Residues6
Detailsbinding site for residue SO4 A 305
ChainResidue
ALYS21
AARG203
ALYS204
AGLU260
AHOH473
AHOH664

site_idAC6
Number of Residues6
Detailsbinding site for residue SO4 A 306
ChainResidue
AARG148
ATRP159
AARG163
AHOH403
AHOH482
AHOH667

site_idAC7
Number of Residues7
Detailsbinding site for residue SO4 A 307
ChainResidue
ASER140
ALYS144
AARG148
AHOH427
AHOH440
AHOH450
AHOH581

site_idAC8
Number of Residues4
Detailsbinding site for residue NA A 308
ChainResidue
AGLU97
AILE100
AASP101
BHOH415

site_idAC9
Number of Residues5
Detailsbinding site for residue NA A 309
ChainResidue
AARG149
AHOH656
BGLU243
BGLN244
BHOH784

site_idAD1
Number of Residues5
Detailsbinding site for residue NA A 310
ChainResidue
ALEU215
AHOH456
BASP248
BHOH721
BHOH772

site_idAD2
Number of Residues13
Detailsbinding site for residue GLU A 311
ChainResidue
ATYR61
APRO89
ALEU90
ATHR91
AARG96
AGLY141
ASER142
ATHR143
AGLU193
ATYR220
AHOH495
AHOH507
AHOH512

site_idAD3
Number of Residues6
Detailsbinding site for residue SO4 B 301
ChainResidue
BARG31
BHOH437
BHOH443
BHOH450
BHOH489
BHOH662

site_idAD4
Number of Residues8
Detailsbinding site for residue SO4 B 302
ChainResidue
BASP139
BSER140
BLYS144
BARG148
BHOH402
BHOH424
BHOH444
BHOH451

site_idAD5
Number of Residues5
Detailsbinding site for residue NA B 303
ChainResidue
BTHR9
BTHR54
BVAL56
BGLU77
BHOH582

site_idAD6
Number of Residues6
Detailsbinding site for residue NA B 304
ChainResidue
BVAL211
BGLY212
BGLY213
BLEU215
BHOH416
BILE113

site_idAD7
Number of Residues13
Detailsbinding site for residue GLU B 305
ChainResidue
BTYR61
BPRO89
BLEU90
BTHR91
BARG96
BGLY141
BSER142
BTHR143
BGLU193
BTYR220
BHOH440
BHOH498
BHOH519

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

224572

PDB entries from 2024-09-04

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