6HDB

Crystal structure of the potassium channel MtTMEM175 with zinc

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0006974	biological_process	DNA damage response
A	0008643	biological_process	carbohydrate transport
A	0015144	molecular_function	carbohydrate transmembrane transporter activity
A	0015768	biological_process	maltose transport
A	0016020	cellular_component	membrane
A	0030288	cellular_component	outer membrane-bounded periplasmic space
A	0034219	biological_process	carbohydrate transmembrane transport
A	0034289	biological_process	detection of maltose stimulus
A	0042597	cellular_component	periplasmic space
A	0042956	biological_process	maltodextrin transmembrane transport
A	0043190	cellular_component	ATP-binding cassette (ABC) transporter complex
A	0055052	cellular_component	ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing
A	0055085	biological_process	transmembrane transport
A	0060326	biological_process	cell chemotaxis
A	1901982	molecular_function	maltose binding
A	1990060	cellular_component	maltose transport complex
B	0005267	molecular_function	potassium channel activity
B	0005886	cellular_component	plasma membrane
B	0015252	molecular_function	proton channel activity
B	0022841	molecular_function	potassium ion leak channel activity
B	0051289	biological_process	protein homotetramerization
B	0071805	biological_process	potassium ion transmembrane transport
B	1902600	biological_process	proton transmembrane transport

Functional Information from PROSITE/UniProt

site_id	PS01037
Number of Residues	18
Details	SBP_BACTERIAL_1 Bacterial extracellular solute-binding proteins, family 1 signature. PIAvEalSLIYNkdlLpN

Chain	Residue	Details
A	PRO224-ASN241

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	139
Details	TRANSMEM: 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

Chain	Residue	Details
B	THR23-SER44
B	SER56-TYR78
B	LYS89-SER117
B	LEU142-TRP165
B	SER187-TRP210
B	THR215-THR237

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site_id	SWS_FT_FI2
Number of Residues	1
Details	SITE: Hydrophobic filter residue 1 => ECO:0000269|PubMed:32267231

Chain	Residue	Details
B	LEU35

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site_id	SWS_FT_FI3
Number of Residues	1
Details	SITE: Hydrophobic filter residue 2 => ECO:0000250|UniProtKB:K9UJK2

Chain	Residue	Details
B	LEU39

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site_id	SWS_FT_FI4
Number of Residues	1
Details	SITE: Hydrophobic filter residue 3 => ECO:0000250|UniProtKB:K9UJK2

Chain	Residue	Details
B	LEU42

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