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3B2L

Iodide derivative of human 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 Residues9
DetailsBINDING SITE FOR RESIDUE PLM A 150
ChainResidue
ASER39
APHE50
AGLU72
APHE95
ATHR102
AILE109
AASN111
AMET113
AARG122

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PLM A 151
ChainResidue
APHE15
ALEU28
AILE52
AALA54
AGLY55
ASER56
ALYS57
AMET74
AASN111
AARG122

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE IOD A 130
ChainResidue
AMET74
AIOD133

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD A 131
ChainResidue
AGLN12

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE IOD A 132
ChainResidue
AGLU40
ALYS49
ATHR51

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE IOD A 133
ChainResidue
ATHR73
AIOD130

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE IOD A 134
ChainResidue
ASER11
AGLU13
AILE123

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

218853

PDB entries from 2024-04-24

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