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8J1H

Agonist1 and Ruthenium Red bound state of mTRPV4

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 Residues564
DetailsTRANSMEM: Helical => ECO:0000250|UniProtKB:O35433
ChainResidueDetails
CSER470-TYR490
DALA573-THR593
DILE609-LEU636
DVAL694-VAL722
BSER470-TYR490
BTYR508-THR534
BSER548-LEU568
BALA573-THR593
BILE609-LEU636
BVAL694-VAL722
ASER470-TYR490
CTYR508-THR534
ATYR508-THR534
ASER548-LEU568
AALA573-THR593
AILE609-LEU636
AVAL694-VAL722
CSER548-LEU568
CALA573-THR593
CILE609-LEU636
CVAL694-VAL722
DSER470-TYR490
DTYR508-THR534
DSER548-LEU568

site_idSWS_FT_FI2
Number of Residues216
DetailsTOPO_DOM: Extracellular => ECO:0000250|UniProtKB:O35433
ChainResidueDetails
CTYR491-ASP507
BALA569-GLU572
BASN637-THR665
BLEU686-VAL693
ATYR491-ASP507
AALA569-GLU572
AASN637-THR665
ALEU686-VAL693
CALA569-GLU572
CASN637-THR665
CLEU686-VAL693
DTYR491-ASP507
DALA569-GLU572
DASN637-THR665
DLEU686-VAL693
BTYR491-ASP507

site_idSWS_FT_FI3
Number of Residues104
DetailsTOPO_DOM: Cytoplasmic => ECO:0000250|UniProtKB:O35433
ChainResidueDetails
CLYS535-GLY547
CARG594-LYS608
DLYS535-GLY547
DARG594-LYS608
BLYS535-GLY547
BARG594-LYS608
ALYS535-GLY547
AARG594-LYS608

site_idSWS_FT_FI4
Number of Residues76
DetailsINTRAMEM: Pore-forming => ECO:0000250|UniProtKB:O35433
ChainResidueDetails
CPHE666-MET685
DPHE666-MET685
BPHE666-MET685
APHE666-MET685

site_idSWS_FT_FI5
Number of Residues20
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9HBA0
ChainResidueDetails
CLYS192
DARG248
BLYS192
BLYS197
BASN201
BTYR236
BARG248
ALYS192
ALYS197
AASN201
ATYR236
CLYS197
AARG248
CASN201
CTYR236
CARG248
DLYS192
DLYS197
DASN201
DTYR236

site_idSWS_FT_FI6
Number of Residues12
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:A0A1D5PXA5
ChainResidueDetails
CARG249
AARG249
AASN296
ALYS344
CASN296
CLYS344
DARG249
DASN296
DLYS344
BARG249
BASN296
BLYS344

site_idSWS_FT_FI7
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9R186
ChainResidueDetails
CASP682
DASP682
BASP682
AASP682

site_idSWS_FT_FI8
Number of Residues4
DetailsMOD_RES: Phosphotyrosine; by LYN => ECO:0000305|PubMed:12538589
ChainResidueDetails
CTYR253
DTYR253
BTYR253
ATYR253

site_idSWS_FT_FI9
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:16368742
ChainResidueDetails
CASN651
DASN651
BASN651
AASN651

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PDB entries from 2024-10-16

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