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7YFF

Structure of GluN1a-GluN2D NMDA receptor in complex with agonist glycine and competitive antagonist CPP.

Functional Information from GO Data
ChainGOidnamespacecontents
A0005216molecular_functionmonoatomic ion channel activity
A0006811biological_processmonoatomic ion transport
A0015276molecular_functionligand-gated monoatomic ion channel activity
A0016020cellular_componentmembrane
A0038023molecular_functionsignaling receptor activity
B0005216molecular_functionmonoatomic ion channel activity
B0006811biological_processmonoatomic ion transport
B0015276molecular_functionligand-gated monoatomic ion channel activity
B0016020cellular_componentmembrane
B0038023molecular_functionsignaling receptor activity
C0005216molecular_functionmonoatomic ion channel activity
C0006811biological_processmonoatomic ion transport
C0015276molecular_functionligand-gated monoatomic ion channel activity
C0016020cellular_componentmembrane
C0038023molecular_functionsignaling receptor activity
D0005216molecular_functionmonoatomic ion channel activity
D0006811biological_processmonoatomic ion transport
D0015276molecular_functionligand-gated monoatomic ion channel activity
D0016020cellular_componentmembrane
D0038023molecular_functionsignaling receptor activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1444
DetailsTOPO_DOM: Extracellular => ECO:0000305|PubMed:36959261
ChainResidueDetails
BPHE28-SER582
BALA675-ASP843
DPHE28-SER582
DALA675-ASP843

site_idSWS_FT_FI2
Number of Residues128
DetailsTRANSMEM: Helical => ECO:0000269|PubMed:36959261
ChainResidueDetails
BPRO583-PHE604
BTHR654-THR674
BASN844-HIS867
DPRO583-PHE604
DTHR654-THR674
DASN844-HIS867

site_idSWS_FT_FI3
Number of Residues70
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:36959261
ChainResidueDetails
BGLU605-ILE629
BASN642-THR653
DGLU605-ILE629
DASN642-THR653

site_idSWS_FT_FI4
Number of Residues22
DetailsINTRAMEM: Discontinuously helical => ECO:0000269|PubMed:36959261
ChainResidueDetails
BGLY630-PHE641
DGLY630-PHE641

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q62645
ChainResidueDetails
BSER539
BTHR718
DSER539
DTHR718

site_idSWS_FT_FI6
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:36959261, ECO:0007744|PDB:7YFR
ChainResidueDetails
BTHR541
BARG546
BSER717
BASP759
DTHR541
DARG546
DSER717
DASP759

site_idSWS_FT_FI7
Number of Residues2
DetailsSITE: Functional determinant of NMDA receptors => ECO:0000250
ChainResidueDetails
BASN642
DASN642

site_idSWS_FT_FI8
Number of Residues12
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
BASN92
DASN384
DASN467
DASN569
BASN352
BASN366
BASN384
BASN467
BASN569
DASN92
DASN352
DASN366

site_idSWS_FT_FI9
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255, ECO:0000269|PubMed:36309015, ECO:0000312|PDB:8E92, ECO:0000312|PDB:8E93, ECO:0000312|PDB:8E94, ECO:0000312|PDB:8E97, ECO:0000312|PDB:8E98, ECO:0000312|PDB:8E99
ChainResidueDetails
AASN61
CASN61

site_idSWS_FT_FI10
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255, ECO:0000269|PubMed:36309015, ECO:0000269|PubMed:36959261, ECO:0000312|PDB:8E92, ECO:0000312|PDB:8E93, ECO:0000312|PDB:8E94, ECO:0000312|PDB:8E97, ECO:0007744|PDB:7YFR
ChainResidueDetails
AASN203
CASN203

site_idSWS_FT_FI11
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255, ECO:0000269|PubMed:36309015, ECO:0000312|PDB:8E93, ECO:0000312|PDB:8E97
ChainResidueDetails
AASN239
CASN239

site_idSWS_FT_FI12
Number of Residues2
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:0007744|PDB:7EOQ
ChainResidueDetails
AASN276
CASN276

site_idSWS_FT_FI13
Number of Residues8
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN300
AASN440
AASN491
AASN674
CASN300
CASN440
CASN491
CASN674

site_idSWS_FT_FI14
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255, ECO:0000269|PubMed:36309015, ECO:0000312|PDB:8E93, ECO:0000312|PDB:8E94, ECO:0000312|PDB:8E96, ECO:0000312|PDB:8E97
ChainResidueDetails
AASN350
CASN350

site_idSWS_FT_FI15
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255, ECO:0000269|PubMed:36309015, ECO:0000312|PDB:8E92, ECO:0000312|PDB:8E94, ECO:0000312|PDB:8E97
ChainResidueDetails
AASN368
CASN368

site_idSWS_FT_FI16
Number of Residues2
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
AASN471
CASN471

site_idSWS_FT_FI17
Number of Residues2
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
AASN771
CASN771

231356

PDB entries from 2025-02-12

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