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6HDC

Crystal structure of the potassium channel MtTMEM175 T38A variant in complex with a Nanobody-MBP fusion protein

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
B0015252molecular_functionproton channel activity
B0022841molecular_functionpotassium ion leak channel activity
B0051289biological_processprotein homotetramerization
B0071805biological_processpotassium ion transmembrane transport
B1902600biological_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 Residues139
DetailsTRANSMEM: Helical => ECO:0000269|PubMed:32267231, ECO:0007744|PDB:6HD8, ECO:0007744|PDB:6HD9, ECO:0007744|PDB:6HDA, ECO:0007744|PDB:6HDB, ECO:0007744|PDB:6HDC, ECO:0007744|PDB:6SWR
ChainResidueDetails
BTHR23-SER44
BSER56-TYR78
BLYS89-SER117
BLEU142-TRP165
BSER187-TRP210
BTHR215-THR237

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: Hydrophobic filter residue 1 => ECO:0000269|PubMed:32267231
ChainResidueDetails
BLEU35

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Hydrophobic filter residue 2 => ECO:0000250|UniProtKB:K9UJK2
ChainResidueDetails
BLEU39

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Hydrophobic filter residue 3 => ECO:0000250|UniProtKB:K9UJK2
ChainResidueDetails
BLEU42

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PDB entries from 2024-07-24

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