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6SWR

Crystal structure of the lysosomal potassium channel MtTMEM175 T38A mutant soaked with zinc

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0006974biological_processDNA damage response
A0008643biological_processcarbohydrate transport
A0015144molecular_functioncarbohydrate transmembrane transporter activity
A0015768biological_processmaltose transport
A0016020cellular_componentmembrane
A0030288cellular_componentouter membrane-bounded periplasmic space
A0034219biological_processcarbohydrate transmembrane transport
A0034289biological_processdetection of maltose stimulus
A0042597cellular_componentperiplasmic space
A0042956biological_processmaltodextrin transmembrane transport
A0043190cellular_componentATP-binding cassette (ABC) transporter complex
A0055052cellular_componentATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing
A0055085biological_processtransmembrane transport
A0060326biological_processcell chemotaxis
A1901982molecular_functionmaltose binding
A1990060cellular_componentmaltose transport complex
B0005267molecular_functionpotassium channel activity
B0005886cellular_componentplasma membrane
B0006811biological_processmonoatomic ion transport
B0006813biological_processpotassium ion transport
B0015252molecular_functionproton channel activity
B0016020cellular_componentmembrane
B0022841molecular_functionpotassium ion leak channel activity
B0034220biological_processmonoatomic ion transmembrane transport
B0051289biological_processprotein homotetramerization
B0071805biological_processpotassium ion transmembrane transport
B1902600biological_processproton transmembrane transport
D0005515molecular_functionprotein binding
D0006974biological_processDNA damage response
D0008643biological_processcarbohydrate transport
D0015144molecular_functioncarbohydrate transmembrane transporter activity
D0015768biological_processmaltose transport
D0016020cellular_componentmembrane
D0030288cellular_componentouter membrane-bounded periplasmic space
D0034219biological_processcarbohydrate transmembrane transport
D0034289biological_processdetection of maltose stimulus
D0042597cellular_componentperiplasmic space
D0042956biological_processmaltodextrin transmembrane transport
D0043190cellular_componentATP-binding cassette (ABC) transporter complex
D0055052cellular_componentATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing
D0055085biological_processtransmembrane transport
D0060326biological_processcell chemotaxis
D1901982molecular_functionmaltose binding
D1990060cellular_componentmaltose transport complex
E0005267molecular_functionpotassium channel activity
E0005886cellular_componentplasma membrane
E0006811biological_processmonoatomic ion transport
E0006813biological_processpotassium ion transport
E0015252molecular_functionproton channel activity
E0016020cellular_componentmembrane
E0022841molecular_functionpotassium ion leak channel activity
E0034220biological_processmonoatomic ion transmembrane transport
E0051289biological_processprotein homotetramerization
E0071805biological_processpotassium ion transmembrane transport
E1902600biological_processproton transmembrane transport
Functional Information from PROSITE/UniProt
site_idPS01037
Number of Residues18
DetailsSBP_BACTERIAL_1 Bacterial extracellular solute-binding proteins, family 1 signature. PIAvEalSLIYNkdlLpN
ChainResidueDetails
APRO224-ASN241

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues256
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"32267231","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6HD8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6HD9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6HDA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6HDB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6HDC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6SWR","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsMotif: {"description":"RxxxFSD motif","evidences":[{"source":"UniProtKB","id":"K9UJK2","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsSite: {"description":"Hydrophobic filter residue 1","evidences":[{"source":"PubMed","id":"32267231","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsSite: {"description":"Hydrophobic filter residue 2","evidences":[{"source":"UniProtKB","id":"K9UJK2","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsSite: {"description":"Hydrophobic filter residue 3","evidences":[{"source":"UniProtKB","id":"K9UJK2","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

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PDB entries from 2025-08-27

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