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1G74

Toward changing specificity: adipocyte lipid binding protein mutant, oleic acid bound form

Functional Information from GO Data
ChainGOidnamespacecontents
A0005324molecular_functionlong-chain fatty acid transmembrane transporter activity
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0008289molecular_functionlipid binding
A0009617biological_processresponse to bacterium
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 Residues8
DetailsBINDING SITE FOR RESIDUE PO4 A 133
ChainResidue
ASER13
AGLU14
AASN15
APHE16
AASP17
AHOH266
AHOH286
AHOH298

site_idAC2
Number of Residues21
DetailsBINDING SITE FOR RESIDUE OLA A 132
ChainResidue
AMET20
AVAL25
AALA33
AALA36
APRO38
AMET40
ASER53
ASER55
APHE57
AVAL75
AASP76
AILE104
AARG106
AVAL115
ACYS117
AARG126
ATYR128
AHOH279
AHOH280
AHOH297
APHE16

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
AVAL127

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N-acetylcysteine => ECO:0000250|UniProtKB:P15090
ChainResidueDetails
AASP2

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21183079
ChainResidueDetails
ASER13

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by Tyr-kinases => ECO:0000250
ChainResidueDetails
AMET20

226707

PDB entries from 2024-10-30

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