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5ELV

Crystal structure of the GluA2 ligand-binding domain (S1S2J-L504-N775) in complex with glutamate and BPAM-521 at 1.92 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 Residues6
Detailsbinding site for residue SO4 A 301
ChainResidue
ASER140
ALYS144
AARG148
AHOH404
AHOH409
AHOH541

site_idAC2
Number of Residues6
Detailsbinding site for residue SO4 A 302
ChainResidue
AHOH456
AHOH461
BLYS183
AARG31
AHOH408
AHOH422

site_idAC3
Number of Residues3
Detailsbinding site for residue SO4 A 303
ChainResidue
AARG149
AHOH474
BLYS240

site_idAC4
Number of Residues4
Detailsbinding site for residue GOL A 304
ChainResidue
AARG148
ATRP159
AARG163
AHOH558

site_idAC5
Number of Residues6
Detailsbinding site for residue GOL A 305
ChainResidue
ASER108
ASER194
ATHR195
AGLU198
AASN214
AHOH465

site_idAC6
Number of Residues2
Detailsbinding site for residue CL A 306
ChainResidue
AARG163
BHOH577

site_idAC7
Number of Residues2
Detailsbinding site for residue CL A 307
ChainResidue
ALYS21
AASN22

site_idAC8
Number of Residues2
Detailsbinding site for residue ACT A 308
ChainResidue
AALA153
BLYS249

site_idAC9
Number of Residues2
Detailsbinding site for residue ACT A 309
ChainResidue
AASP257
AHOH431

site_idAD1
Number of Residues4
Detailsbinding site for residue ACT A 310
ChainResidue
AASP248
BASN214
BASP216
BSER217

site_idAD2
Number of Residues5
Detailsbinding site for residue ACT A 311
ChainResidue
AASP38
AGLU42
ALEU250
ALYS253
BLYS21

site_idAD3
Number of Residues13
Detailsbinding site for residue 5PX A 312
ChainResidue
APRO105
ASER108
ASER217
ALYS218
AGLY219
AHOH545
BLYS104
BPRO105
BPHE106
BMET107
BSER108
BSER242
B5PX312

site_idAD4
Number of Residues12
Detailsbinding site for residue GLU A 313
ChainResidue
ATYR61
APRO89
ALEU90
ATHR91
AARG96
AGLY141
ASER142
ATHR143
AGLU193
AHOH437
AHOH444
AHOH473

site_idAD5
Number of Residues6
Detailsbinding site for residue SO4 B 301
ChainResidue
BSER140
BLYS144
BARG148
BHOH411
BHOH430
BHOH458

site_idAD6
Number of Residues5
Detailsbinding site for residue GOL B 302
ChainResidue
BSER108
BSER194
BGLU198
BASN214
BHOH407

site_idAD7
Number of Residues4
Detailsbinding site for residue GOL B 303
ChainResidue
BARG148
BTRP159
BARG163
BACT307

site_idAD8
Number of Residues2
Detailsbinding site for residue CL B 304
ChainResidue
BLYS4
BTHR5

site_idAD9
Number of Residues2
Detailsbinding site for residue ACT B 305
ChainResidue
BLYS82
BLYS116

site_idAE1
Number of Residues3
Detailsbinding site for residue ACT B 306
ChainResidue
BASP58
BLYS60
BASN72

site_idAE2
Number of Residues3
Detailsbinding site for residue ACT B 307
ChainResidue
BLYS144
BARG163
BGOL303

site_idAE3
Number of Residues4
Detailsbinding site for residue ACT B 308
ChainResidue
BSER123
BALA124
BGLY213
BHOH422

site_idAE4
Number of Residues5
Detailsbinding site for residue ACT B 309
ChainResidue
BLYS240
BHOH504
ATYR94
BHIS46
BALA237

site_idAE5
Number of Residues5
Detailsbinding site for residue PEG B 310
ChainResidue
BGLU27
BGLY28
BARG31
BLYS52
BHOH453

site_idAE6
Number of Residues4
Detailsbinding site for residue PEG B 311
ChainResidue
AARG203
ALYS258
BHIS23
BARG31

site_idAE7
Number of Residues12
Detailsbinding site for residue 5PX B 312
ChainResidue
ALYS104
APRO105
APHE106
AMET107
ASER108
ASER242
A5PX312
BPRO105
BSER108
BSER217
BLYS218
BGLY219

site_idAE8
Number of Residues12
Detailsbinding site for residue GLU B 313
ChainResidue
BTYR61
BPRO89
BLEU90
BTHR91
BARG96
BGLY141
BSER142
BTHR143
BGLU193
BHOH462
BHOH465
BHOH467

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

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PDB entries from 2024-07-24

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