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3STK

Crystal Structure of human LFABP complex with two molecules of palmitic acid (holo-LFABP)

Functional Information from GO Data
ChainGOidnamespacecontents
A0003682molecular_functionchromatin binding
A0005324molecular_functionlong-chain fatty acid transmembrane transporter activity
A0005504molecular_functionfatty acid binding
A0005515molecular_functionprotein binding
A0005543molecular_functionphospholipid binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005782cellular_componentperoxisomal matrix
A0005829cellular_componentcytosol
A0008289molecular_functionlipid binding
A0015908biological_processfatty acid transport
A0015909biological_processlong-chain fatty acid transport
A0016209molecular_functionantioxidant activity
A0032000biological_processpositive regulation of fatty acid beta-oxidation
A0032052molecular_functionbile acid binding
A0032991cellular_componentprotein-containing complex
A0033552biological_processresponse to vitamin B3
A0043066biological_processnegative regulation of apoptotic process
A0043154biological_processnegative regulation of cysteine-type endopeptidase activity involved in apoptotic process
A0045179cellular_componentapical cortex
A0050892biological_processintestinal absorption
A0070062cellular_componentextracellular exosome
A0070301biological_processcellular response to hydrogen peroxide
A0070538molecular_functionoleic acid binding
A0071456biological_processcellular response to hypoxia
A0098869biological_processcellular oxidant detoxification
A1901363molecular_functionheterocyclic compound binding
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PLM A 130
ChainResidue
ASER39
AILE52
AGLU72
ATHR102
AASN111
AARG122
APLM131
AHOH227

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PLM A 131
ChainResidue
ASER56
AASN111
AARG122
APLM130
AALA54

Functional Information from PROSITE/UniProt
site_idPS00214
Number of Residues18
DetailsFABP Cytosolic fatty-acid binding proteins signature. GKYqLqsQeNFEaFMKAI
ChainResidueDetails
AGLY5-ILE22

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER11
ASER56

site_idSWS_FT_FI2
Number of Residues7
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P12710
ChainResidueDetails
ALYS31
ALYS36
ALYS46
ALYS57
ALYS78
ALYS90
ALYS121

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P02692
ChainResidueDetails
ASER39

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ATHR51

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P12710
ChainResidueDetails
ASER100

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PDB entries from 2024-10-30

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