Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

8G8W

Molecular mechanism of nucleotide inhibition of human uncoupling protein 1

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0002024	biological_process	diet induced thermogenesis
A	0005525	molecular_function	GTP binding
A	0005739	cellular_component	mitochondrion
A	0005740	cellular_component	mitochondrial envelope
A	0005743	cellular_component	mitochondrial inner membrane
A	0006811	biological_process	monoatomic ion transport
A	0006839	biological_process	mitochondrial transport
A	0009266	biological_process	response to temperature stimulus
A	0009409	biological_process	response to cold
A	0015078	molecular_function	proton transmembrane transporter activity
A	0017077	molecular_function	oxidative phosphorylation uncoupler activity
A	0019003	molecular_function	GDP binding
A	0022857	molecular_function	transmembrane transporter activity
A	0031667	biological_process	response to nutrient levels
A	0032555	molecular_function	purine ribonucleotide binding
A	0032870	biological_process	cellular response to hormone stimulus
A	0034220	biological_process	monoatomic ion transmembrane transport
A	0034614	biological_process	cellular response to reactive oxygen species
A	0036041	molecular_function	long-chain fatty acid binding
A	0043168	molecular_function	anion binding
A	0050873	biological_process	brown fat cell differentiation
A	0055085	biological_process	transmembrane transport
A	0070417	biological_process	cellular response to cold
A	0071398	biological_process	cellular response to fatty acid
A	0120162	biological_process	positive regulation of cold-induced thermogenesis
A	1901612	molecular_function	cardiolipin binding
A	1902600	biological_process	proton transmembrane transport
A	1903426	biological_process	regulation of reactive oxygen species biosynthetic process
A	1903495	biological_process	cellular response to dehydroepiandrosterone
A	1990542	biological_process	mitochondrial transmembrane transport
A	1990845	biological_process	adaptive thermogenesis
B	0005515	molecular_function	protein binding
B	0006974	biological_process	DNA damage response
B	0008643	biological_process	carbohydrate transport
B	0015144	molecular_function	carbohydrate transmembrane transporter activity
B	0015768	biological_process	maltose transport
B	0016020	cellular_component	membrane
B	0030288	cellular_component	outer membrane-bounded periplasmic space
B	0034219	biological_process	carbohydrate transmembrane transport
B	0034289	biological_process	detection of maltose stimulus
B	0042597	cellular_component	periplasmic space
B	0042956	biological_process	maltodextrin transmembrane transport
B	0043190	cellular_component	ATP-binding cassette (ABC) transporter complex
B	0055052	cellular_component	ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing
B	0055085	biological_process	transmembrane transport
B	0060326	biological_process	cell chemotaxis
B	1901982	molecular_function	maltose binding
C	0005515	molecular_function	protein binding
C	0006974	biological_process	DNA damage response
C	0008643	biological_process	carbohydrate transport
C	0015144	molecular_function	carbohydrate transmembrane transporter activity
C	0015768	biological_process	maltose transport
C	0016020	cellular_component	membrane
C	0030288	cellular_component	outer membrane-bounded periplasmic space
C	0034219	biological_process	carbohydrate transmembrane transport
C	0034289	biological_process	detection of maltose stimulus
C	0042597	cellular_component	periplasmic space
C	0042956	biological_process	maltodextrin transmembrane transport
C	0043190	cellular_component	ATP-binding cassette (ABC) transporter complex
C	0055052	cellular_component	ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing
C	0055085	biological_process	transmembrane transport
C	0060326	biological_process	cell chemotaxis
C	1901982	molecular_function	maltose binding

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
B	PRO228-ASN245
C	PRO232-ASN249

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	21
Details	Transmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	117
Details	Topological domain: {"description":"Mitochondrial matrix","evidences":[{"source":"UniProtKB","id":"P04633","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	22
Details	Transmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	35
Details	Topological domain: {"description":"Mitochondrial intermembrane","evidences":[{"source":"UniProtKB","id":"P04633","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	16
Details	Transmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	16
Details	Transmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	19
Details	Transmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	22
Details	Transmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	91
Details	Repeat: {"description":"Solcar 1"}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	90
Details	Repeat: {"description":"Solcar 2"}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	85
Details	Repeat: {"description":"Solcar 3"}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"28781081","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	1
Details	Modified residue: {"description":"Cysteine sulfenic acid (-SOH)","evidences":[{"source":"UniProtKB","id":"P12242","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)