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2Q9S

Linoleic Acid Bound to Fatty Acid Binding Protein 4

Functional Information from GO Data
ChainGOidnamespacecontents
A0005324molecular_functionlong-chain fatty acid transmembrane transporter activity
A0005504molecular_functionfatty acid binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006631biological_processfatty acid metabolic process
A0008284biological_processpositive regulation of cell population proliferation
A0008289molecular_functionlipid binding
A0009617biological_processresponse to bacterium
A0015908biological_processfatty acid transport
A0015909biological_processlong-chain fatty acid transport
A0036041molecular_functionlong-chain fatty acid binding
A0042632biological_processcholesterol homeostasis
A0045892biological_processnegative regulation of DNA-templated transcription
A0050729biological_processpositive regulation of inflammatory response
A0050872biological_processwhite fat cell differentiation
A0050873biological_processbrown fat cell differentiation
A0051427molecular_functionhormone receptor binding
A0071285biological_processcellular response to lithium ion
A0071356biological_processcellular response to tumor necrosis factor
A0120162biological_processpositive regulation of cold-induced thermogenesis
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 501
ChainResidue
AARG108
AARG108
AGLY110
AGLY110
AASP111
AASP111
AARG130
AARG130
AHOH630

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE EIC A 601
ChainResidue
AVAL25
AALA33
APRO38
ASER53
APHE57
AASP76
AVAL115
ACYS117
AARG126
ATYR128

Functional Information from PROSITE/UniProt
site_idPS00214
Number of Residues18
DetailsFABP Cytosolic fatty-acid binding proteins signature. GTWkLvsSeNFDdYMKEV
ChainResidueDetails
AGLY6-VAL23

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING:
ChainResidueDetails
AARG126

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N-acetylcysteine => ECO:0000250|UniProtKB:P15090
ChainResidueDetails
ACYS1

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21183079
ChainResidueDetails
ASER12

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by Tyr-kinases => ECO:0000250
ChainResidueDetails
ATYR19

219869

PDB entries from 2024-05-15

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