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9B69

GluA2 flip Q in complex with TARPgamma2 at pH8, class12, structure of NTD

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2780
DetailsTOPO_DOM: Extracellular
ChainResidueDetails
CVAL7-ALA528
CTHR623-ASN797
AVAL7-ALA528
ATHR623-ASN797
BVAL7-ALA528
BTHR623-ASN797
DVAL7-ALA528
DTHR623-ASN797

site_idSWS_FT_FI2
Number of Residues160
DetailsTRANSMEM: Helical
ChainResidueDetails
CTYR529-VAL549
CLEU602-TYR622
ATYR529-VAL549
ALEU602-TYR622
BTYR529-VAL549
BLEU602-TYR622
DTYR529-VAL549
DLEU602-TYR622

site_idSWS_FT_FI3
Number of Residues320
DetailsTOPO_DOM: Cytoplasmic
ChainResidueDetails
CSER550-GLU576
DSER550-GLU576
DASP596-SER601
DGLU819-GLY868
CASP596-SER601
CGLU819-GLY868
ASER550-GLU576
AASP596-SER601
AGLU819-GLY868
BSER550-GLU576
BASP596-SER601
BGLU819-GLY868

site_idSWS_FT_FI4
Number of Residues60
DetailsINTRAMEM: Helical; Pore-forming
ChainResidueDetails
CPHE577-GLN592
APHE577-GLN592
BPHE577-GLN592
DPHE577-GLN592

site_idSWS_FT_FI5
Number of Residues8
DetailsINTRAMEM:
ChainResidueDetails
CGLN593-CYS595
AGLN593-CYS595
BGLN593-CYS595
DGLN593-CYS595

site_idSWS_FT_FI6
Number of Residues80
DetailsTRANSMEM: Helical; Name=M4
ChainResidueDetails
CVAL798-ILE818
AVAL798-ILE818
BVAL798-ILE818
DVAL798-ILE818

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
CPRO484
ASER660
ATHR661
AGLU711
BPRO484
BTHR486
BARG491
BSER660
BTHR661
BGLU711
DPRO484
CTHR486
DTHR486
DARG491
DSER660
DTHR661
DGLU711
CARG491
CSER660
CTHR661
CGLU711
APRO484
ATHR486
AARG491

site_idSWS_FT_FI8
Number of Residues12
DetailsSITE: Interaction with the cone snail toxin Con-ikot-ikot => ECO:0000269|PubMed:25103405
ChainResidueDetails
CARG459
DARG459
DARG666
DLYS758
CARG666
CLYS758
AARG459
AARG666
ALYS758
BARG459
BARG666
BLYS758

site_idSWS_FT_FI9
Number of Residues4
DetailsSITE: Crucial to convey clamshell closure to channel opening => ECO:0000269|PubMed:25103405
ChainResidueDetails
CILE639
AILE639
BILE639
DILE639

site_idSWS_FT_FI10
Number of Residues4
DetailsMOD_RES: Phosphoserine; by PKC => ECO:0000269|PubMed:8848293
ChainResidueDetails
CSER668
ASER668
BSER668
DSER668

site_idSWS_FT_FI11
Number of Residues4
DetailsMOD_RES: Phosphoserine; by PKG => ECO:0000269|PubMed:8848293
ChainResidueDetails
CSER702
ASER702
BSER702
DSER702

site_idSWS_FT_FI12
Number of Residues12
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P23819
ChainResidueDetails
CSER845
DSER845
DSER848
DASN865
CSER848
CASN865
ASER845
ASER848
AASN865
BSER845
BSER848
BASN865

site_idSWS_FT_FI13
Number of Residues4
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:15240807, ECO:0000269|PubMed:20547133
ChainResidueDetails
CLYS861
ALYS861
BLYS861
DLYS861

site_idSWS_FT_FI14
Number of Residues8
DetailsLIPID: S-palmitoyl cysteine => ECO:0000250
ChainResidueDetails
CCYS595
CCYS821
ACYS595
ACYS821
BCYS595
BCYS821
DCYS595
DCYS821

site_idSWS_FT_FI15
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:21317873
ChainResidueDetails
CASN241
AASN241
BASN241
DASN241

site_idSWS_FT_FI16
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19946266, ECO:0000269|PubMed:21317873, ECO:0000269|PubMed:25103405
ChainResidueDetails
CASN355
AASN355
BASN355
DASN355

site_idSWS_FT_FI17
Number of Residues8
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
CASN391
CASN398
AASN391
AASN398
BASN391
BASN398
DASN391
DASN398

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PDB entries from 2024-07-31

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