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5H8Q

Structure of the human GluN1/GluN2A LBD in complex with GNE8324

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 Residues1
Detailsbinding site for residue ACT A 301
ChainResidue
AARG39

site_idAC2
Number of Residues11
Detailsbinding site for residue GLU A 302
ChainResidue
AASP214
AHOH448
AHOH472
AHIS87
ASER113
ATHR115
AARG120
AGLY171
ASER172
ATHR173
ATYR213

site_idAC3
Number of Residues7
Detailsbinding site for residue GLY B 301
ChainResidue
BPHE93
BPRO125
BTHR127
BARG132
BSER180
BSER181
BASP225

site_idAC4
Number of Residues16
Detailsbinding site for residue 5YE B 302
ChainResidue
AILE116
APRO129
AVAL131
AGLU132
ATHR241
ATHR242
AGLY243
AVAL266
BLYS140
BPRO141
BLYS143
BTYR144
BGLY250
BLEU270
BHIS273
BHOH401

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:26875626, ECO:0000269|PubMed:26919761, ECO:0000269|PubMed:28105280, ECO:0007744|PDB:5H8F, ECO:0007744|PDB:5H8H, ECO:0007744|PDB:5H8N, ECO:0007744|PDB:5H8Q, ECO:0007744|PDB:5I2K, ECO:0007744|PDB:5I2N, ECO:0007744|PDB:5KCJ, ECO:0007744|PDB:5KDT, ECO:0007744|PDB:5TP9, ECO:0007744|PDB:5TPA
ChainResidueDetails
BPRO125
BARG132
BSER181
BASP225

site_idSWS_FT_FI2
Number of Residues5
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
BASN49
BASN80
BASN100
BASN167
BASN264

site_idSWS_FT_FI3
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN45
AASN46
AASN170

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PDB entries from 2024-07-17

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