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9W62

Cryo-EM structure of human ABCD3 in inward-facing conformation in the presence of phytanoyl-CoA

Functional Information from GO Data
ChainGOidnamespacecontents
B0000038biological_processvery long-chain fatty acid metabolic process
B0005324molecular_functionlong-chain fatty acid transmembrane transporter activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005739cellular_componentmitochondrion
B0005777cellular_componentperoxisome
B0005778cellular_componentperoxisomal membrane
B0005782cellular_componentperoxisomal matrix
B0005829cellular_componentcytosol
B0006091biological_processgeneration of precursor metabolites and energy
B0006633biological_processfatty acid biosynthetic process
B0006635biological_processfatty acid beta-oxidation
B0006699biological_processbile acid biosynthetic process
B0006869biological_processlipid transport
B0007031biological_processperoxisome organization
B0008218biological_processbioluminescence
B0009410biological_processresponse to xenobiotic stimulus
B0015721biological_processbile acid and bile salt transport
B0015910biological_processlong-chain fatty acid import into peroxisome
B0016020cellular_componentmembrane
B0016887molecular_functionATP hydrolysis activity
B0042626molecular_functionATPase-coupled transmembrane transporter activity
B0042760biological_processvery long-chain fatty acid catabolic process
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0047617molecular_functionfatty acyl-CoA hydrolase activity
B0052817molecular_functionvery long-chain fatty acyl-CoA hydrolase activity
B1903512biological_processphytanic acid metabolic process
Functional Information from PROSITE/UniProt
site_idPS00211
Number of Residues15
DetailsABC_TRANSPORTER_1 ABC transporters family signature. LSGGEKQRMAMARLF
ChainResidueDetails
BLEU571-PHE585

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues80
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues287
DetailsDomain: {"description":"ABC transmembrane type-1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P55096","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

256448

PDB entries from 2026-07-15

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