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2XXR

Crystal structure of the GluK2 (GluR6) wild-type LBD dimer 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 Residues13
DetailsBINDING SITE FOR RESIDUE GLU A 900
ChainResidue
ATYR488
AHOH2072
AHOH2126
AHOH2185
AHOH2255
APRO516
ALEU517
AALA518
AARG523
AGLY688
AALA689
ATHR690
AGLU738

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE GLU B 900
ChainResidue
BTYR488
BPRO516
BLEU517
BALA518
BARG523
BGLY688
BALA689
BTHR690
BGLU738
BHOH2116
BHOH2153
BHOH2220
BHOH2221

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 901
ChainResidue
ALYS531
AARG775
AHOH2231
BLYS531
BARG775

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 902
ChainResidue
AGLU524
AILE527
AASP528
AHOH2104

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA B 902
ChainResidue
BGLU524
BILE527
BASP528
BMET770
BHOH2084

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15721240","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17115050","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1S50","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1S7Y","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2I0B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2I0C","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"15677325","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8163463","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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