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7FXL

Crystal Structure of human FABP4 binding site mutated to that of FABP5 in complex with myristic acid

Functional Information from GO Data
ChainGOidnamespacecontents
A0005319molecular_functionlipid transporter activity
A0005324molecular_functionlong-chain fatty acid transmembrane transporter activity
A0005504molecular_functionfatty acid binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005811cellular_componentlipid droplet
A0005829cellular_componentcytosol
A0008289molecular_functionlipid binding
A0015908biological_processfatty acid transport
A0015909biological_processlong-chain fatty acid transport
A0019433biological_processtriglyceride catabolic process
A0036041molecular_functionlong-chain fatty acid binding
A0051427molecular_functionhormone receptor binding
A0060229molecular_functionlipase activator activity
A0070062cellular_componentextracellular exosome
A0070343biological_processwhite fat cell proliferation
A0120162biological_processpositive regulation of cold-induced thermogenesis
Functional Information from PROSITE/UniProt
site_idPS00214
Number of Residues18
DetailsFABP Cytosolic fatty-acid binding proteins signature. GTWkLvsSeNFDdYMKEL
ChainResidueDetails
AGLY6-LEU23

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsMotif: {"description":"Nuclear localization signal","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P04117","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine; by Tyr-kinases","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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