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5H8N

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

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 Residues10
Detailsbinding site for residue GLU A 301
ChainResidue
AHIS87
AHOH438
ASER113
ATHR115
AARG120
AGLY171
ASER172
ATHR173
AASP214
AHOH402

site_idAC2
Number of Residues13
Detailsbinding site for residue 5YD A 302
ChainResidue
APRO129
APHE130
AVAL131
AGLU132
ALEU263
AVAL266
AMET271
AGLU275
AHOH424
BPRO141
BARG248
BSER249
BGLY250

site_idAC3
Number of Residues9
Detailsbinding site for residue GLY B 302
ChainResidue
BPHE93
BPRO125
BLEU126
BTHR127
BARG132
BSER180
BSER181
BASP225
BPHE251

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
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
ATHR115
AARG120
ASER172
ATHR173

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:26875626, ECO:0000269|PubMed:26919761, ECO:0000269|PubMed:28105280, ECO:0000269|PubMed:36959261, 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, ECO:0007744|PDB:7YFF
ChainResidueDetails
BTHR127
BSER181

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:26875626, ECO:0000269|PubMed:26919761, ECO:0000269|PubMed:28105280, ECO:0000269|PubMed:36309015, ECO:0000269|PubMed:36959261, ECO:0000312|PDB:8E96, 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, ECO:0007744|PDB:7YFR
ChainResidueDetails
BARG132
AASN46

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:26875626, ECO:0000269|PubMed:26919761, ECO:0000269|PubMed:28105280, ECO:0000269|PubMed:36309015, ECO:0000269|PubMed:36959261, ECO:0000312|PDB:8E96, 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, ECO:0007744|PDB:7YFF
ChainResidueDetails
BASP225

site_idSWS_FT_FI5
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
BASN49
BASN100
BASN167

site_idSWS_FT_FI6
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255, ECO:0000269|PubMed:34186027, ECO:0000269|PubMed:36309015, ECO:0000269|PubMed:36959261, ECO:0000312|PDB:8E93, ECO:0000312|PDB:8E94, ECO:0000312|PDB:8E97, ECO:0000312|PDB:8E98, ECO:0007744|PDB:7EOQ, ECO:0007744|PDB:7YFR
ChainResidueDetails
BASN80

site_idSWS_FT_FI7
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255, ECO:0000269|PubMed:34186027, ECO:0000269|PubMed:36309015, ECO:0000312|PDB:8E92, ECO:0000312|PDB:8E93, ECO:0000312|PDB:8E94, ECO:0000312|PDB:8E96, ECO:0000312|PDB:8E97, ECO:0000312|PDB:8E98, ECO:0000312|PDB:8E99, ECO:0007744|PDB:7EOQ
ChainResidueDetails
BASN264

237423

PDB entries from 2025-06-11

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