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2XHD

Crystal structure of N-((2S)-5-(6-fluoro-3-pyridinyl)-2,3-dihydro-1H- inden-2-yl)-2-propanesulfonamide in complex with the ligand binding domain of the human GluA2 receptor

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 Residues13
DetailsBINDING SITE FOR RESIDUE GLU A 301
ChainResidue
ATYR61
ATYR220
AHOH2148
AHOH2205
AHOH2283
APRO89
ALEU90
ATHR91
AARG96
AGLY141
ASER142
ATHR143
AGLU193

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 1264
ChainResidue
ASER140
ALYS144
AARG148
AHOH2150
AHOH2284
AHOH2285
AHOH2286

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 1265
ChainResidue
AARG148
ATRP159
AARG163

site_idAC4
Number of Residues13
DetailsBINDING SITE FOR RESIDUE GLU B 301
ChainResidue
BTYR61
BPRO89
BLEU90
BTHR91
BARG96
BGLY141
BSER142
BTHR143
BGLU193
BTYR220
BHOH2138
BHOH2185
BHOH2245

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 B 1263
ChainResidue
BASP139
BSER140
BLYS144
BARG148
BHOH2081
BHOH2246
BHOH2247
BHOH2248

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 1264
ChainResidue
ALYS183
BARG31
BHOH2040
BHOH2249
BHOH2250

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 1265
ChainResidue
BARG148
BTRP159
BARG163
BHOH2251

site_idAC8
Number of Residues26
DetailsBINDING SITE FOR RESIDUE 7T9 B 1266
ChainResidue
ALYS104
APRO105
AMET107
ASER108
ASER217
ALYS218
AGLY219
ASER242
AHOH2234
AHOH2257
BLYS104
BPRO105
BMET107
BSER108
BSER217
BLYS218
BGLY219
BSER242
BHOH3000
BHOH3001
BHOH3002
BHOH3003
BHOH3004
BHOH3005
BHOH3006
BHOH3007

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues80
DetailsTRANSMEM: Helical => ECO:0000250
ChainResidueDetails
AALA134-VAL154
AASP207-GLY227
BALA134-VAL154
BASP207-GLY227

site_idSWS_FT_FI2
Number of Residues62
DetailsTOPO_DOM: Cytoplasmic => ECO:0000250
ChainResidueDetails
APHE155-VAL181
AGLU201-CYS206
BPHE155-VAL181
BGLU201-CYS206

site_idSWS_FT_FI3
Number of Residues30
DetailsINTRAMEM: Helical; Pore-forming => ECO:0000250
ChainResidueDetails
AARG182-ASN197
BARG182-ASN197

site_idSWS_FT_FI4
Number of Residues4
DetailsINTRAMEM: INTRAMEM => ECO:0000250
ChainResidueDetails
AGLU198-ILE200
BGLU198-ILE200

site_idSWS_FT_FI5
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:20614889, ECO:0007744|PDB:2XHD
ChainResidueDetails
APRO89
ATHR91
ASER142
ATHR143
BPRO89
BTHR91
BSER142
BTHR143

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:20614889, ECO:0000269|PubMed:21531559, ECO:0007744|PDB:2XHD, ECO:0007744|PDB:3R7X
ChainResidueDetails
AARG96
BARG96

site_idSWS_FT_FI7
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:20614889, ECO:0000269|PubMed:21531559, ECO:0007744|PDB:2XHD
ChainResidueDetails
AGLU193
BGLU193

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PKC => ECO:0000250|UniProtKB:P19491
ChainResidueDetails
ASER150
BSER150

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PKG => ECO:0000250|UniProtKB:P19491
ChainResidueDetails
ASER184
BSER184

site_idSWS_FT_FI10
Number of Residues2
DetailsLIPID: S-palmitoyl cysteine => ECO:0000250
ChainResidueDetails
AILE200
BILE200

site_idSWS_FT_FI11
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN3
BASN3

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PDB entries from 2024-07-31

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