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24VE

Structure of cytosol-open ABCD4-LMBD1

Functional Information from GO Data
ChainGOidnamespacecontents
A0005324molecular_functionlong-chain fatty acid transmembrane transporter activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005765cellular_componentlysosomal membrane
A0005777cellular_componentperoxisome
A0005778cellular_componentperoxisomal membrane
A0005789cellular_componentendoplasmic reticulum membrane
A0006635biological_processfatty acid beta-oxidation
A0007031biological_processperoxisome organization
A0009235biological_processcobalamin metabolic process
A0015420molecular_functionABC-type vitamin B12 transporter activity
A0015889biological_processcobalamin transport
A0015910biological_processlong-chain fatty acid import into peroxisome
A0016020cellular_componentmembrane
A0042626molecular_functionATPase-coupled transmembrane transporter activity
A0042760biological_processvery long-chain fatty acid catabolic process
A0042802molecular_functionidentical protein binding
A0043190cellular_componentATP-binding cassette (ABC) transporter complex
A0055085biological_processtransmembrane transport
B0005324molecular_functionlong-chain fatty acid transmembrane transporter activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005765cellular_componentlysosomal membrane
B0005777cellular_componentperoxisome
B0005778cellular_componentperoxisomal membrane
B0005789cellular_componentendoplasmic reticulum membrane
B0006635biological_processfatty acid beta-oxidation
B0007031biological_processperoxisome organization
B0009235biological_processcobalamin metabolic process
B0015420molecular_functionABC-type vitamin B12 transporter activity
B0015889biological_processcobalamin transport
B0015910biological_processlong-chain fatty acid import into peroxisome
B0016020cellular_componentmembrane
B0042626molecular_functionATPase-coupled transmembrane transporter activity
B0042760biological_processvery long-chain fatty acid catabolic process
B0042802molecular_functionidentical protein binding
B0043190cellular_componentATP-binding cassette (ABC) transporter complex
B0055085biological_processtransmembrane transport
C0005158molecular_functioninsulin receptor binding
C0005515molecular_functionprotein binding
C0005764cellular_componentlysosome
C0005765cellular_componentlysosomal membrane
C0005789cellular_componentendoplasmic reticulum membrane
C0005886cellular_componentplasma membrane
C0007369biological_processgastrulation
C0015420molecular_functionABC-type vitamin B12 transporter activity
C0015889biological_processcobalamin transport
C0016020cellular_componentmembrane
C0030136cellular_componentclathrin-coated vesicle
C0032050molecular_functionclathrin heavy chain binding
C0035461biological_processvitamin transmembrane transport
C0035612molecular_functionAP-2 adaptor complex binding
C0038016biological_processinsulin receptor internalization
C0045334cellular_componentclathrin-coated endocytic vesicle
C0061462biological_processprotein localization to lysosome
C0072583biological_processclathrin-dependent endocytosis
C0090482molecular_functionvitamin transmembrane transporter activity
Functional Information from PROSITE/UniProt
site_idPS00211
Number of Residues15
DetailsABC_TRANSPORTER_1 ABC transporters family signature. LSPGEMQRLSFARLF
ChainResidueDetails
ALEU524-PHE538

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues200
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues586
DetailsDomain: {"description":"ABC transmembrane type-1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues428
DetailsDomain: {"description":"ABC transporter","evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues135
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues28
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=8","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=9","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues3
DetailsMotif: {"description":"YERL motif; mediates interaction with adapter protein complex 2 and is essential for its function in clathrin-mediated endocytosis of INSR","evidences":[{"source":"UniProtKB","id":"Q8K0B2","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues3
DetailsMotif: {"description":"WTKF motif; mediates interaction with adapter protein complex 2 and is essential for its function in clathrin-mediated endocytosis of INSR","evidences":[{"source":"UniProtKB","id":"Q8K0B2","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q8K0B2","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

258009

PDB entries from 2026-08-12

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