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3STM

Structure of human LFABP in complex with one molecule of palmitic acid

Functional Information from GO Data
ChainGOidnamespacecontents
X0003682molecular_functionchromatin binding
X0005324molecular_functionlong-chain fatty acid transmembrane transporter activity
X0005504molecular_functionfatty acid binding
X0005515molecular_functionprotein binding
X0005543molecular_functionphospholipid binding
X0005634cellular_componentnucleus
X0005654cellular_componentnucleoplasm
X0005737cellular_componentcytoplasm
X0005782cellular_componentperoxisomal matrix
X0005829cellular_componentcytosol
X0008289molecular_functionlipid binding
X0015908biological_processfatty acid transport
X0015909biological_processlong-chain fatty acid transport
X0016209molecular_functionantioxidant activity
X0032000biological_processpositive regulation of fatty acid beta-oxidation
X0032052molecular_functionbile acid binding
X0032991cellular_componentprotein-containing complex
X0033552biological_processresponse to vitamin B3
X0043066biological_processnegative regulation of apoptotic process
X0043154biological_processnegative regulation of cysteine-type endopeptidase activity involved in apoptotic process
X0045179cellular_componentapical cortex
X0050892biological_processintestinal absorption
X0070062cellular_componentextracellular exosome
X0070301biological_processcellular response to hydrogen peroxide
X0070538molecular_functionoleic acid binding
X0071456biological_processcellular response to hypoxia
X0098869biological_processcellular oxidant detoxification
X1901363molecular_functionheterocyclic compound binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PLM X 130
ChainResidue
XSER39
XPHE50
XGLU72
XTHR102
XASN111
XARG122
XHOH132

Functional Information from PROSITE/UniProt
site_idPS00214
Number of Residues18
DetailsFABP Cytosolic fatty-acid binding proteins signature. GKYqLqsQeNFEaFMKAI
ChainResidueDetails
XGLY5-ILE22

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
XSER11
XSER56

site_idSWS_FT_FI2
Number of Residues7
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P12710
ChainResidueDetails
XLYS31
XLYS36
XLYS46
XLYS57
XLYS78
XLYS90
XLYS121

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P02692
ChainResidueDetails
XSER39

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569
ChainResidueDetails
XTHR51

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P12710
ChainResidueDetails
XSER100

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PDB entries from 2024-05-01

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