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5VRE

Crystal structure of a lysosomal potassium-selective channel TMEM175 homolog from Chamaesiphon Minutus

Functional Information from GO Data
ChainGOidnamespacecontents
A0005267molecular_functionpotassium channel activity
A0006811biological_processmonoatomic ion transport
A0006813biological_processpotassium ion transport
A0015252molecular_functionproton channel activity
A0016020cellular_componentmembrane
A0034220biological_processmonoatomic ion transmembrane transport
A0042802molecular_functionidentical protein binding
A0051289biological_processprotein homotetramerization
A0071805biological_processpotassium ion transmembrane transport
A1902600biological_processproton transmembrane transport
B0005267molecular_functionpotassium channel activity
B0006811biological_processmonoatomic ion transport
B0006813biological_processpotassium ion transport
B0015252molecular_functionproton channel activity
B0016020cellular_componentmembrane
B0034220biological_processmonoatomic ion transmembrane transport
B0042802molecular_functionidentical protein binding
B0051289biological_processprotein homotetramerization
B0071805biological_processpotassium ion transmembrane transport
B1902600biological_processproton transmembrane transport
C0005267molecular_functionpotassium channel activity
C0006811biological_processmonoatomic ion transport
C0006813biological_processpotassium ion transport
C0015252molecular_functionproton channel activity
C0016020cellular_componentmembrane
C0034220biological_processmonoatomic ion transmembrane transport
C0042802molecular_functionidentical protein binding
C0051289biological_processprotein homotetramerization
C0071805biological_processpotassium ion transmembrane transport
C1902600biological_processproton transmembrane transport
D0005267molecular_functionpotassium channel activity
D0006811biological_processmonoatomic ion transport
D0006813biological_processpotassium ion transport
D0015252molecular_functionproton channel activity
D0016020cellular_componentmembrane
D0034220biological_processmonoatomic ion transmembrane transport
D0042802molecular_functionidentical protein binding
D0051289biological_processprotein homotetramerization
D0071805biological_processpotassium ion transmembrane transport
D1902600biological_processproton transmembrane transport
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues100
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:28723891
ChainResidueDetails
AMET1-GLN7
CLEU79-ASP84
CALA143-ASP154
CARG200-ALA203
DMET1-GLN7
DLEU79-ASP84
DALA143-ASP154
DARG200-ALA203
ALEU79-ASP84
AALA143-ASP154
AARG200-ALA203
BMET1-GLN7
BLEU79-ASP84
BALA143-ASP154
BARG200-ALA203
CMET1-GLN7

site_idSWS_FT_FI2
Number of Residues92
DetailsTRANSMEM: Helical; Name=TM1 => ECO:0000269|PubMed:28723891
ChainResidueDetails
ASER8-GLU31
BSER8-GLU31
CSER8-GLU31
DSER8-GLU31

site_idSWS_FT_FI3
Number of Residues108
DetailsTOPO_DOM: Extracellular => ECO:0000305|PubMed:28723891
ChainResidueDetails
AILE32-LEU52
DILE32-LEU52
DTYR111-ALA117
DSER182-VAL183
ATYR111-ALA117
ASER182-VAL183
BILE32-LEU52
BTYR111-ALA117
BSER182-VAL183
CILE32-LEU52
CTYR111-ALA117
CSER182-VAL183

site_idSWS_FT_FI4
Number of Residues100
DetailsTRANSMEM: Helical; Name=TM2 => ECO:0000269|PubMed:28723891
ChainResidueDetails
ATRP53-SER78
BTRP53-SER78
CTRP53-SER78
DTRP53-SER78

site_idSWS_FT_FI5
Number of Residues100
DetailsTRANSMEM: Helical; Name=TM3 => ECO:0000269|PubMed:28723891
ChainResidueDetails
AHIS85-GLU110
BHIS85-GLU110
CHIS85-GLU110
DHIS85-GLU110

site_idSWS_FT_FI6
Number of Residues96
DetailsTRANSMEM: Helical; Name=TM4 => ECO:0000269|PubMed:28723891
ChainResidueDetails
AARG118-ALA142
BARG118-ALA142
CARG118-ALA142
DARG118-ALA142

site_idSWS_FT_FI7
Number of Residues104
DetailsTRANSMEM: Helical; Name=TM5 => ECO:0000269|PubMed:28723891
ChainResidueDetails
AARG155-ILE181
BARG155-ILE181
CARG155-ILE181
DARG155-ILE181

site_idSWS_FT_FI8
Number of Residues60
DetailsTRANSMEM: Helical; Name=TM6 => ECO:0000269|PubMed:28723891
ChainResidueDetails
ATRP184-LEU199
BTRP184-LEU199
CTRP184-LEU199
DTRP184-LEU199

site_idSWS_FT_FI9
Number of Residues4
DetailsSITE: Hydrophobic filter residue 1 => ECO:0000269|PubMed:28723891
ChainResidueDetails
AILE23
BILE23
CILE23
DILE23

site_idSWS_FT_FI10
Number of Residues4
DetailsSITE: Hydrophobic filter residue 2 => ECO:0000269|PubMed:28723891
ChainResidueDetails
ALEU27
BLEU27
CLEU27
DLEU27

site_idSWS_FT_FI11
Number of Residues4
DetailsSITE: Hydrophobic filter residue 3 => ECO:0000269|PubMed:28723891
ChainResidueDetails
ALEU30
BLEU30
CLEU30
DLEU30

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PDB entries from 2024-04-24

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