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3RNN

Crystal Structure of iGluR2 Ligand Binding Domain with Symmetric Sulfonamide Containing Potentiator

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 Residues10
DetailsBINDING SITE FOR RESIDUE RNN A 280
ChainResidue
ALYS104
CGLY219
APRO105
ASER108
ALYS218
AGLY219
ALEU239
CLYS104
CPRO105
CLYS218

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE GLU A 281
ChainResidue
ATYR61
APRO89
ALEU90
ATHR91
AARG96
AGLY141
ASER142
ATHR143
AGLU193
AHOH286
AHOH287
AHOH294

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN A 282
ChainResidue
AGLU42
AHIS46
BGLU166

site_idAC4
Number of Residues13
DetailsBINDING SITE FOR RESIDUE RNN B 280
ChainResidue
BLYS104
BLYS104
BPRO105
BPRO105
BSER108
BSER108
BLYS218
BLYS218
BGLY219
BGLY219
BLEU239
BLEU239
BASN242

site_idAC5
Number of Residues13
DetailsBINDING SITE FOR RESIDUE GLU B 281
ChainResidue
BTYR61
BPRO89
BLEU90
BTHR91
BARG96
BLEU138
BGLY141
BSER142
BTHR143
BGLU193
BHOH288
BHOH304
BHOH311

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 282
ChainResidue
BHIS23
BGLU30
CHIS23
CGLU24

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 283
ChainResidue
AGLU166
BGLU42
BHIS46
BLEU241
BHOH478

site_idAC8
Number of Residues13
DetailsBINDING SITE FOR RESIDUE GLU C 280
ChainResidue
CTYR61
CPRO89
CLEU90
CTHR91
CARG96
CLEU138
CGLY141
CSER142
CTHR143
CGLU193
CHOH283
CHOH297
CHOH321

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 281
ChainResidue
AHIS23
CASP65
CHOH490
CHOH491

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 282
ChainResidue
CGLU42
CLYS45
CHIS46
CHOH806

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:20614889, ECO:0007744|PDB:2XHD
ChainResidueDetails
APRO89
CTHR91
CSER142
CTHR143
ATHR91
ASER142
ATHR143
BPRO89
BTHR91
BSER142
BTHR143
CPRO89

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:20614889, ECO:0000269|PubMed:21531559, ECO:0007744|PDB:2XHD, ECO:0007744|PDB:3R7X
ChainResidueDetails
AARG96
BARG96
CARG96

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:20614889, ECO:0000269|PubMed:21531559, ECO:0007744|PDB:2XHD
ChainResidueDetails
AGLU193
BGLU193
CGLU193

site_idSWS_FT_FI4
Number of Residues3
DetailsMOD_RES: Phosphoserine; by PKC => ECO:0000250|UniProtKB:P19491
ChainResidueDetails
ASER150
BSER150
CSER150

site_idSWS_FT_FI5
Number of Residues3
DetailsMOD_RES: Phosphoserine; by PKG => ECO:0000250|UniProtKB:P19491
ChainResidueDetails
ASER184
BSER184
CSER184

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

223532

PDB entries from 2024-08-07

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