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7P5C

Cryo-EM structure of human TTYH3 in Ca2+ and GDN

Functional Information from GO Data
ChainGOidnamespacecontents
A0005225molecular_functionvolume-sensitive anion channel activity
A0005229molecular_functionintracellularly calcium-gated chloride channel activity
A0005254molecular_functionchloride channel activity
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005886cellular_componentplasma membrane
A0006821biological_processchloride transport
A0016020cellular_componentmembrane
A0034220biological_processmonoatomic ion transmembrane transport
A0034707cellular_componentchloride channel complex
A0046872molecular_functionmetal ion binding
A0070062cellular_componentextracellular exosome
A0072320molecular_functionvolume-sensitive chloride channel activity
A1902476biological_processchloride transmembrane transport
B0005225molecular_functionvolume-sensitive anion channel activity
B0005229molecular_functionintracellularly calcium-gated chloride channel activity
B0005254molecular_functionchloride channel activity
B0005509molecular_functioncalcium ion binding
B0005515molecular_functionprotein binding
B0005886cellular_componentplasma membrane
B0006821biological_processchloride transport
B0016020cellular_componentmembrane
B0034220biological_processmonoatomic ion transmembrane transport
B0034707cellular_componentchloride channel complex
B0046872molecular_functionmetal ion binding
B0070062cellular_componentextracellular exosome
B0072320molecular_functionvolume-sensitive chloride channel activity
B1902476biological_processchloride transmembrane transport
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues40
DetailsTRANSMEM: Helical; Name=1 => ECO:0000255
ChainResidueDetails
ALEU43-PHE63
BLEU43-PHE63

site_idSWS_FT_FI2
Number of Residues280
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:18260827
ChainResidueDetails
AARG233-LYS236
ASER408-HIS523
BTYR64-THR86
BARG233-LYS236
BSER408-HIS523
ATYR64-THR86

site_idSWS_FT_FI3
Number of Residues40
DetailsTRANSMEM: Helical; Name=2 => ECO:0000255
ChainResidueDetails
AALA87-GLY107
BALA87-GLY107

site_idSWS_FT_FI4
Number of Residues462
DetailsTOPO_DOM: Extracellular => ECO:0000305|PubMed:18260827
ChainResidueDetails
AASN108-LEU211
AGLY258-GLU386
BASN108-LEU211
BGLY258-GLU386

site_idSWS_FT_FI5
Number of Residues40
DetailsTRANSMEM: Helical; Name=3 => ECO:0000255
ChainResidueDetails
AGLY212-ILE232
BGLY212-ILE232

site_idSWS_FT_FI6
Number of Residues40
DetailsTRANSMEM: Helical; Name=4 => ECO:0000255
ChainResidueDetails
AGLY237-LEU257
BGLY237-LEU257

site_idSWS_FT_FI7
Number of Residues40
DetailsTRANSMEM: Helical; Name=5 => ECO:0000255
ChainResidueDetails
AGLY387-CYS407
BGLY387-CYS407

site_idSWS_FT_FI8
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q6P5F7
ChainResidueDetails
BASP113
AGLU110
AASP113
BGLU110

site_idSWS_FT_FI9
Number of Residues2
DetailsSITE: Essential for the formation of the channel-pore => ECO:0000250|UniProtKB:Q9D3A9
ChainResidueDetails
AARG161
BARG161

site_idSWS_FT_FI10
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q6P5F7
ChainResidueDetails
ASER496
BSER496
BSER504
ASER504

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692
ChainResidueDetails
ASER522
BSER522

site_idSWS_FT_FI12
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:34385445
ChainResidueDetails
AASN126
BASN126

site_idSWS_FT_FI13
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:34385445
ChainResidueDetails
AASN144
BASN144

site_idSWS_FT_FI14
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:18260827, ECO:0000269|PubMed:34385445, ECO:0000305|PubMed:15010458
ChainResidueDetails
AASN351
BASN351

221051

PDB entries from 2024-06-12

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