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7P54

Cryo-EM structure of human TTYH2 in 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
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
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
ALEU45-ALA65
BLEU45-ALA65

site_idSWS_FT_FI2
Number of Residues300
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:18260827
ChainResidueDetails
ATYR66-CYS87
AALA235-CYS240
AGLY410-ALA534
BTYR66-CYS87
BALA235-CYS240
BGLY410-ALA534

site_idSWS_FT_FI3
Number of Residues40
DetailsTRANSMEM: Helical; Name=2 => ECO:0000255
ChainResidueDetails
ACYS88-PHE108
BCYS88-PHE108

site_idSWS_FT_FI4
Number of Residues460
DetailsTOPO_DOM: Extracellular => ECO:0000305|PubMed:18260827
ChainResidueDetails
ATYR109-TRP213
AALA262-GLY388
BTYR109-TRP213
BALA262-GLY388

site_idSWS_FT_FI5
Number of Residues40
DetailsTRANSMEM: Helical; Name=3 => ECO:0000255
ChainResidueDetails
ALEU214-LEU234
BLEU214-LEU234

site_idSWS_FT_FI6
Number of Residues40
DetailsTRANSMEM: Helical; Name=4 => ECO:0000255
ChainResidueDetails
ALEU241-ALA261
BLEU241-ALA261

site_idSWS_FT_FI7
Number of Residues40
DetailsTRANSMEM: Helical; Name=5 => ECO:0000255
ChainResidueDetails
ALEU389-ALA409
BLEU389-ALA409

site_idSWS_FT_FI8
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q3TH73
ChainResidueDetails
AGLU113
AASP116
BGLU113
BASP116

site_idSWS_FT_FI9
Number of Residues2
DetailsSITE: Essential for the formation of the channel-pore => ECO:0000250|UniProtKB:Q3TH73
ChainResidueDetails
AARG164
BARG164

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:17081983
ChainResidueDetails
ATHR199
BTHR199

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q3TH73
ChainResidueDetails
ASER504
BSER504

site_idSWS_FT_FI12
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:18260827, ECO:0000269|PubMed:34385445
ChainResidueDetails
AASN31
AASN283
BASN31
BASN283

site_idSWS_FT_FI13
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc) asparagine => ECO:0000269|PubMed:18260827, ECO:0000269|PubMed:34385445
ChainResidueDetails
AASN129
AASN352
BASN129
BASN352

222415

PDB entries from 2024-07-10

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