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6BWI

3.7 angstrom cryoEM structure of full length human TRPM4

Functional Information from GO Data
ChainGOidnamespacecontents
A0005216molecular_functionmonoatomic ion channel activity
A0006811biological_processmonoatomic ion transport
A0016020cellular_componentmembrane
A0055085biological_processtransmembrane transport
B0005216molecular_functionmonoatomic ion channel activity
B0006811biological_processmonoatomic ion transport
B0016020cellular_componentmembrane
B0055085biological_processtransmembrane transport
C0005216molecular_functionmonoatomic ion channel activity
C0006811biological_processmonoatomic ion transport
C0016020cellular_componentmembrane
C0055085biological_processtransmembrane transport
D0005216molecular_functionmonoatomic ion channel activity
D0006811biological_processmonoatomic ion transport
D0016020cellular_componentmembrane
D0055085biological_processtransmembrane transport
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues492
DetailsTRANSMEM: Helical => ECO:0000269|PubMed:29211723, ECO:0000269|PubMed:29217581
ChainResidueDetails
APHE783-VAL803
BLEU887-PHE910
BPHE931-LEU951
BVAL1020-ILE1040
CPHE783-VAL803
CLEU815-GLY835
CTRP864-THR884
CLEU887-PHE910
CPHE931-LEU951
CVAL1020-ILE1040
DPHE783-VAL803
ALEU815-GLY835
DLEU815-GLY835
DTRP864-THR884
DLEU887-PHE910
DPHE931-LEU951
DVAL1020-ILE1040
ATRP864-THR884
ALEU887-PHE910
APHE931-LEU951
AVAL1020-ILE1040
BPHE783-VAL803
BLEU815-GLY835
BTRP864-THR884

site_idSWS_FT_FI2
Number of Residues224
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:29211723, ECO:0000269|PubMed:29217581
ChainResidueDetails
AASP804-GLU814
CPRO885-GLY886
CLEU952-LEU963
CVAL985-LEU1019
DASP804-GLU814
DPRO885-GLY886
DLEU952-LEU963
DVAL985-LEU1019
APRO885-GLY886
ALEU952-LEU963
AVAL985-LEU1019
BASP804-GLU814
BPRO885-GLY886
BLEU952-LEU963
BVAL985-LEU1019
CASP804-GLU814

site_idSWS_FT_FI3
Number of Residues184
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:29211723, ECO:0000269|PubMed:29217581
ChainResidueDetails
AGLY836-SER863
ATHR911-VAL930
BGLY836-SER863
BTHR911-VAL930
CGLY836-SER863
CTHR911-VAL930
DGLY836-SER863
DTHR911-VAL930

site_idSWS_FT_FI4
Number of Residues80
DetailsINTRAMEM: Pore-forming => ECO:0000269|PubMed:29211723, ECO:0000269|PubMed:29217581
ChainResidueDetails
AARG964-ASP984
BARG964-ASP984
CARG964-ASP984
DARG964-ASP984

site_idSWS_FT_FI5
Number of Residues8
DetailsBINDING: in other chain => ECO:0000250|UniProtKB:Q7TN37
ChainResidueDetails
AARG421
AGLY448
BARG421
BGLY448
CARG421
CGLY448
DARG421
DGLY448

site_idSWS_FT_FI6
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:29217581, ECO:0007744|PDB:6BQV
ChainResidueDetails
AGLU828
DGLU828
DGLN831
DASN865
AGLN831
AASN865
BGLU828
BGLN831
BASN865
CGLU828
CGLN831
CASN865

site_idSWS_FT_FI7
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305|PubMed:29217581, ECO:0007744|PDB:6BQV
ChainResidueDetails
AASP868
BASP868
CASP868
DASP868

site_idSWS_FT_FI8
Number of Residues8
DetailsMOD_RES: Phosphoserine; by PKC => ECO:0000305|PubMed:15590641
ChainResidueDetails
ASER1145
ASER1152
BSER1145
BSER1152
CSER1145
CSER1152
DSER1145
DSER1152

site_idSWS_FT_FI9
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:29217581
ChainResidueDetails
AASN992
BASN992
CASN992
DASN992

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PDB entries from 2024-07-24

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