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5KCJ

Structure of the human GluN1/GluN2A LBD in complex with GNE6901

Replaces:  5H8R
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 Residues2
Detailsbinding site for residue ACT A 301
ChainResidue
AARG39
ATYR80

site_idAC2
Number of Residues12
Detailsbinding site for residue GLU A 302
ChainResidue
ATHR173
ATYR213
AASP214
AHOH432
AHOH477
AHIS87
ASER113
ALEU114
ATHR115
AARG120
AGLY171
ASER172

site_idAC3
Number of Residues9
Detailsbinding site for residue GLY B 301
ChainResidue
BPHE93
BPRO125
BLEU126
BTHR127
BARG132
BSER180
BSER181
BASP225
BPHE251

site_idAC4
Number of Residues18
Detailsbinding site for residue 6RM B 302
ChainResidue
AILE116
APRO129
APHE130
AVAL131
AGLU132
ATHR241
ATHR242
AGLY243
AVAL266
BILE128
BLYS140
BPRO141
BTYR144
BGLY250
BLEU270
BHIS273
BHOH462
BHOH467

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
BLYS104
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
BGLU106
BILE160

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
BMET111
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
BTYR204

site_idSWS_FT_FI5
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
BTHR28
BMET79

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
BTHR59

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
BGLY243

237735

PDB entries from 2025-06-18

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