8Z0F

Cryo-EM structure of ATP-bound human very long-chain fatty acid ABC transporter ABCD3

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000038	biological_process	very long-chain fatty acid metabolic process
A	0000166	molecular_function	nucleotide binding
A	0005324	molecular_function	long-chain fatty acid transmembrane transporter activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005739	cellular_component	mitochondrion
A	0005777	cellular_component	peroxisome
A	0005778	cellular_component	peroxisomal membrane
A	0005782	cellular_component	peroxisomal matrix
A	0005829	cellular_component	cytosol
A	0006633	biological_process	fatty acid biosynthetic process
A	0006635	biological_process	fatty acid beta-oxidation
A	0006699	biological_process	bile acid biosynthetic process
A	0006869	biological_process	lipid transport
A	0007031	biological_process	peroxisome organization
A	0009410	biological_process	response to xenobiotic stimulus
A	0015721	biological_process	bile acid and bile salt transport
A	0015910	biological_process	long-chain fatty acid import into peroxisome
A	0016020	cellular_component	membrane
A	0016787	molecular_function	hydrolase activity
A	0016887	molecular_function	ATP hydrolysis activity
A	0042626	molecular_function	ATPase-coupled transmembrane transporter activity
A	0042760	biological_process	very long-chain fatty acid catabolic process
A	0042802	molecular_function	identical protein binding
A	0042803	molecular_function	protein homodimerization activity
A	0047617	molecular_function	fatty acyl-CoA hydrolase activity
A	0055085	biological_process	transmembrane transport
A	0140359	molecular_function	ABC-type transporter activity
A	1903512	biological_process	phytanic acid metabolic process
B	0000038	biological_process	very long-chain fatty acid metabolic process
B	0000166	molecular_function	nucleotide binding
B	0005324	molecular_function	long-chain fatty acid transmembrane transporter activity
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005739	cellular_component	mitochondrion
B	0005777	cellular_component	peroxisome
B	0005778	cellular_component	peroxisomal membrane
B	0005782	cellular_component	peroxisomal matrix
B	0005829	cellular_component	cytosol
B	0006633	biological_process	fatty acid biosynthetic process
B	0006635	biological_process	fatty acid beta-oxidation
B	0006699	biological_process	bile acid biosynthetic process
B	0006869	biological_process	lipid transport
B	0007031	biological_process	peroxisome organization
B	0009410	biological_process	response to xenobiotic stimulus
B	0015721	biological_process	bile acid and bile salt transport
B	0015910	biological_process	long-chain fatty acid import into peroxisome
B	0016020	cellular_component	membrane
B	0016787	molecular_function	hydrolase activity
B	0016887	molecular_function	ATP hydrolysis activity
B	0042626	molecular_function	ATPase-coupled transmembrane transporter activity
B	0042760	biological_process	very long-chain fatty acid catabolic process
B	0042802	molecular_function	identical protein binding
B	0042803	molecular_function	protein homodimerization activity
B	0047617	molecular_function	fatty acyl-CoA hydrolase activity
B	0055085	biological_process	transmembrane transport
B	0140359	molecular_function	ABC-type transporter activity
B	1903512	biological_process	phytanic acid metabolic process

Functional Information from PROSITE/UniProt

site_id	PS00211
Number of Residues	15
Details	ABC_TRANSPORTER_1 ABC transporters family signature. LSGGEKQRMAMARLF

Chain	Residue	Details
A	LEU571-PHE585

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	120
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	14
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P55096","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---