Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5L1G

AMPA subtype ionotropic glutamate receptor GluA2 in complex with GYKI-Br

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 Residues160
DetailsTRANSMEM: Helical
ChainResidueDetails
AILE529-THR568
ALEU596-TYR616
BILE529-THR568
BLEU596-TYR616
CILE529-THR568
CLEU596-TYR616
DILE529-THR568
DLEU596-TYR616

site_idSWS_FT_FI2
Number of Residues60
DetailsINTRAMEM: Helical; Pore-forming
ChainResidueDetails
APHE571-GLN586
BPHE571-GLN586
CPHE571-GLN586
DPHE571-GLN586

site_idSWS_FT_FI3
Number of Residues8
DetailsINTRAMEM:
ChainResidueDetails
AGLN587-ALA589
BGLN587-ALA589
CGLN587-ALA589
DGLN587-ALA589

site_idSWS_FT_FI4
Number of Residues20
DetailsTOPO_DOM: Cytoplasmic
ChainResidueDetails
AASP590-SER595
BASP590-SER595
CASP590-SER595
DASP590-SER595

site_idSWS_FT_FI5
Number of Residues696
DetailsTOPO_DOM: Extracellular
ChainResidueDetails
ATHR617-ASN791
BTHR617-ASN791
CTHR617-ASN791
DTHR617-ASN791

site_idSWS_FT_FI6
Number of Residues80
DetailsTRANSMEM: Helical; Name=M4
ChainResidueDetails
AVAL792-ILE812
BVAL792-ILE812
CVAL792-ILE812
DVAL792-ILE812

site_idSWS_FT_FI7
Number of Residues24
DetailsBINDING: BINDING => ECO:0000269|PubMed:11086992, ECO:0000269|PubMed:16483599, ECO:0007744|PDB:1FTJ, ECO:0007744|PDB:2CMO
ChainResidueDetails
ATHR655
AGLU705
BVAL484
BGLU486
BPHE491
BSER654
BTHR655
BGLU705
CVAL484
CGLU486
CPHE491
CSER654
CTHR655
CGLU705
DVAL484
DGLU486
DPHE491
DSER654
DTHR655
DGLU705
AVAL484
AGLU486
APHE491
ASER654

site_idSWS_FT_FI8
Number of Residues12
DetailsSITE: Interaction with the cone snail toxin Con-ikot-ikot => ECO:0000269|PubMed:25103405
ChainResidueDetails
DILE459
DARG660
DLYS752
BARG660
BLYS752
CILE459
CARG660
CLYS752
AILE459
AARG660
ALYS752
BILE459

site_idSWS_FT_FI9
Number of Residues4
DetailsSITE: Crucial to convey clamshell closure to channel opening => ECO:0000269|PubMed:25103405
ChainResidueDetails
AILE633
BILE633
CILE633
DILE633

site_idSWS_FT_FI10
Number of Residues4
DetailsMOD_RES: Phosphoserine; by PKC => ECO:0000269|PubMed:8848293
ChainResidueDetails
ASER662
BSER662
CSER662
DSER662

site_idSWS_FT_FI11
Number of Residues4
DetailsMOD_RES: Phosphoserine; by PKG => ECO:0000269|PubMed:8848293
ChainResidueDetails
ASER696
BSER696
CSER696
DSER696

site_idSWS_FT_FI12
Number of Residues8
DetailsLIPID: S-palmitoyl cysteine => ECO:0000250
ChainResidueDetails
CALA589
CCYS815
DALA589
DCYS815
AALA589
ACYS815
BALA589
BCYS815

site_idSWS_FT_FI13
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:21317873
ChainResidueDetails
AGLU241
BGLU241
CGLU241
DGLU241

site_idSWS_FT_FI14
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19946266, ECO:0000269|PubMed:21317873, ECO:0000269|PubMed:25103405
ChainResidueDetails
AASN355
BASN355
CASN355
DASN355

site_idSWS_FT_FI15
Number of Residues8
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
CGLU391
CTHR398
DGLU391
DTHR398
AGLU391
ATHR398
BGLU391
BTHR398

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon