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5OEW

Crystal structure of the GluA2 ligand-binding domain (S1S2J) in complex with glutamate and positive allosteric modulator BPAM538

Functional Information from GO Data
ChainGOidnamespacecontents
A0015276molecular_functionligand-gated monoatomic ion channel activity
A0016020cellular_componentmembrane
B0015276molecular_functionligand-gated monoatomic ion channel activity
B0016020cellular_componentmembrane
C0015276molecular_functionligand-gated monoatomic ion channel activity
C0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue GLU A 301
ChainResidue
ATYR61
AHOH434
AHOH442
AHOH447
APRO89
ALEU90
ATHR91
AARG96
AGLY141
ASER142
ATHR143
AGLU193

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN A 302
ChainResidue
AGLU42
AHIS46
AHOH546
CGLU166

site_idAC3
Number of Residues1
Detailsbinding site for residue ZN A 303
ChainResidue
AASP126

site_idAC4
Number of Residues2
Detailsbinding site for residue ZN A 304
ChainResidue
AHOH407
AHOH411

site_idAC5
Number of Residues3
Detailsbinding site for residue ACT A 305
ChainResidue
AASP216
ASER217
BASP248

site_idAC6
Number of Residues26
Detailsbinding site for residue 9TE B 901
ChainResidue
ALYS104
APRO105
APHE106
AMET107
ASER108
ASER217
ALYS218
AGLY219
AASN242
ALEU247
AHOH416
AHOH470
AHOH553
AHOH554
BLYS104
BPRO105
BPHE106
BMET107
BSER108
BSER217
BLYS218
BGLY219
BASN242
BLEU247
BHOH1053
BHOH1069

site_idAC7
Number of Residues13
Detailsbinding site for residue GLU B 902
ChainResidue
BTYR61
BPRO89
BLEU90
BTHR91
BARG96
BLEU138
BGLY141
BSER142
BTHR143
BGLU193
BHOH1015
BHOH1043
BHOH1061

site_idAC8
Number of Residues5
Detailsbinding site for residue ZN B 903
ChainResidue
BGLU42
BLYS45
BHIS46
BHOH1063
BHOH1140

site_idAC9
Number of Residues2
Detailsbinding site for residue ZN B 904
ChainResidue
BASP139
BHOH1017

site_idAD1
Number of Residues4
Detailsbinding site for residue ZN B 905
ChainResidue
BASP156
BHOH1052
BHOH1124
BHOH1133

site_idAD2
Number of Residues3
Detailsbinding site for residue ZN B 906
ChainResidue
BASP65
BACT909
BHOH1122

site_idAD3
Number of Residues2
Detailsbinding site for residue ZN B 907
ChainResidue
BHIS46
BHOH1158

site_idAD4
Number of Residues2
Detailsbinding site for residue ZN B 908
ChainResidue
BHOH1006
BHOH1007

site_idAD5
Number of Residues4
Detailsbinding site for residue ACT B 909
ChainResidue
BASP65
BASP67
BZN906
BHOH1008

site_idAD6
Number of Residues18
Detailsbinding site for residue 9TE C 301
ChainResidue
CHOH402
CHOH403
CLYS104
CPRO105
CPRO105
CPHE106
CPHE106
CMET107
CMET107
CSER108
CSER217
CLYS218
CLYS218
CGLY219
CASN242
CASN242
CLEU247
CHOH401

site_idAD7
Number of Residues12
Detailsbinding site for residue GLU C 302
ChainResidue
CTYR61
CPRO89
CLEU90
CTHR91
CARG96
CGLY141
CSER142
CTHR143
CGLU193
CHOH433
CHOH467
CHOH484

site_idAD8
Number of Residues4
Detailsbinding site for residue ZN C 303
ChainResidue
CHIS46
CHOH510
CHOH580
CHOH584

site_idAD9
Number of Residues3
Detailsbinding site for residue ZN C 304
ChainResidue
CASP156
CHOH415
CHOH578

site_idAE1
Number of Residues3
Detailsbinding site for residue ZN C 305
ChainResidue
CHIS23
CGLU30
CACT312

site_idAE2
Number of Residues4
Detailsbinding site for residue ZN C 306
ChainResidue
CGLU42
CHIS46
CLEU241
CHOH422

site_idAE3
Number of Residues2
Detailsbinding site for residue ZN C 307
ChainResidue
CHOH407
CHOH458

site_idAE4
Number of Residues2
Detailsbinding site for residue ZN C 308
ChainResidue
CASP126
CHOH525

site_idAE5
Number of Residues1
Detailsbinding site for residue ZN C 309
ChainResidue
CGLU132

site_idAE6
Number of Residues2
Detailsbinding site for residue ZN C 310
ChainResidue
CHOH404
CHOH421

site_idAE7
Number of Residues3
Detailsbinding site for residue ACT C 311
ChainResidue
CARG180
CSER184
CLYS187

site_idAE8
Number of Residues5
Detailsbinding site for residue ACT C 312
ChainResidue
CLYS20
CHIS23
CGLU30
CZN305
CHOH480

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues18
DetailsBINDING: BINDING => ECO:0000269|PubMed:11086992, ECO:0000269|PubMed:16483599, ECO:0007744|PDB:1FTJ, ECO:0007744|PDB:2CMO
ChainResidueDetails
APRO89
BSER142
BTHR143
BGLU193
CPRO89
CTHR91
CARG96
CSER142
CTHR143
CGLU193
ATHR91
AARG96
ASER142
ATHR143
AGLU193
BPRO89
BTHR91
BARG96

site_idSWS_FT_FI2
Number of Residues9
DetailsSITE: Interaction with the cone snail toxin Con-ikot-ikot => ECO:0000269|PubMed:25103405
ChainResidueDetails
AARG64
AARG148
ALYS240
BARG64
BARG148
BLYS240
CARG64
CARG148
CLYS240

site_idSWS_FT_FI3
Number of Residues3
DetailsSITE: Crucial to convey clamshell closure to channel opening => ECO:0000269|PubMed:25103405
ChainResidueDetails
AILE121
BILE121
CILE121

site_idSWS_FT_FI4
Number of Residues3
DetailsMOD_RES: Phosphoserine; by PKC => ECO:0000269|PubMed:8848293
ChainResidueDetails
ASER150
BSER150
CSER150

site_idSWS_FT_FI5
Number of Residues3
DetailsMOD_RES: Phosphoserine; by PKG => ECO:0000269|PubMed:8848293
ChainResidueDetails
ASER184
BSER184
CSER184

site_idSWS_FT_FI6
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN3
BASN3
CASN3

227111

PDB entries from 2024-11-06

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