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6U5S

NTD of GluA2 in complex with CNIH3 - with antagonist ZK200775 - in pseudo-symmetric global conformation

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 Residues2780
DetailsTOPO_DOM: Extracellular
ChainResidueDetails
AVAL7-ALA528
ATHR623-ASN797
BVAL7-ALA528
BTHR623-ASN797
CVAL7-ALA528
CTHR623-ASN797
DVAL7-ALA528
DTHR623-ASN797

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

site_idSWS_FT_FI3
Number of Residues124
DetailsTOPO_DOM: Cytoplasmic
ChainResidueDetails
ASER550-GLU576
AASP596-SER601
BSER550-GLU576
BASP596-SER601
CSER550-GLU576
CASP596-SER601
DSER550-GLU576
DASP596-SER601

site_idSWS_FT_FI4
Number of Residues60
DetailsINTRAMEM: Helical; Pore-forming
ChainResidueDetails
APHE577-ARG592
BPHE577-ARG592
CPHE577-ARG592
DPHE577-ARG592

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

site_idSWS_FT_FI6
Number of Residues80
DetailsTRANSMEM: Helical; Name=M4
ChainResidueDetails
AVAL798-ILE818
BVAL798-ILE818
CVAL798-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
APRO484
BSER660
BTHR661
BGLU711
CPRO484
CTHR486
CARG491
CSER660
CTHR661
CGLU711
DPRO484
ATHR486
DTHR486
DARG491
DSER660
DTHR661
DGLU711
AARG491
ASER660
ATHR661
AGLU711
BPRO484
BTHR486
BARG491

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

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

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

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

site_idSWS_FT_FI12
Number of Residues8
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P23819
ChainResidueDetails
ASER845
ASER848
BSER845
BSER848
CSER845
CSER848
DSER845
DSER848

site_idSWS_FT_FI13
Number of Residues8
DetailsLIPID: S-palmitoyl cysteine => ECO:0000250
ChainResidueDetails
ACYS595
ACYS821
BCYS595
BCYS821
CCYS595
CCYS821
DCYS595
DCYS821

site_idSWS_FT_FI14
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:21317873
ChainResidueDetails
AASN241
BASN241
CASN241
DASN241

site_idSWS_FT_FI15
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_FI16
Number of Residues8
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN391
AASN398
BASN391
BASN398
CASN391
CASN398
DASN391
DASN398

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PDB entries from 2024-10-30

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