Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

7FWI

Crystal Structure of human FABP5 in complex with 2-(indole-1-carbonylamino)benzoic acid

Functional Information from GO Data
ChainGOidnamespacecontents
A0001972molecular_functionretinoic acid binding
A0005324molecular_functionlong-chain fatty acid transmembrane transporter activity
A0005504molecular_functionfatty acid binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006006biological_processglucose metabolic process
A0006629biological_processlipid metabolic process
A0006656biological_processphosphatidylcholine biosynthetic process
A0006869biological_processlipid transport
A0008289molecular_functionlipid binding
A0008544biological_processepidermis development
A0010829biological_processnegative regulation of glucose transmembrane transport
A0014069cellular_componentpostsynaptic density
A0015908biological_processfatty acid transport
A0015909biological_processlong-chain fatty acid transport
A0030667cellular_componentsecretory granule membrane
A0031392biological_processregulation of prostaglandin biosynthetic process
A0035360biological_processpositive regulation of peroxisome proliferator activated receptor signaling pathway
A0035578cellular_componentazurophil granule lumen
A0042593biological_processglucose homeostasis
A0042802molecular_functionidentical protein binding
A0045202cellular_componentsynapse
A0051930biological_processregulation of sensory perception of pain
A0070062cellular_componentextracellular exosome
A0099178biological_processregulation of retrograde trans-synaptic signaling by endocanabinoid
A0120162biological_processpositive regulation of cold-induced thermogenesis
A1990379biological_processlipid transport across blood-brain barrier
B0001972molecular_functionretinoic acid binding
B0005324molecular_functionlong-chain fatty acid transmembrane transporter activity
B0005504molecular_functionfatty acid binding
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006006biological_processglucose metabolic process
B0006629biological_processlipid metabolic process
B0006656biological_processphosphatidylcholine biosynthetic process
B0006869biological_processlipid transport
B0008289molecular_functionlipid binding
B0008544biological_processepidermis development
B0010829biological_processnegative regulation of glucose transmembrane transport
B0014069cellular_componentpostsynaptic density
B0015908biological_processfatty acid transport
B0015909biological_processlong-chain fatty acid transport
B0030667cellular_componentsecretory granule membrane
B0031392biological_processregulation of prostaglandin biosynthetic process
B0035360biological_processpositive regulation of peroxisome proliferator activated receptor signaling pathway
B0035578cellular_componentazurophil granule lumen
B0042593biological_processglucose homeostasis
B0042802molecular_functionidentical protein binding
B0045202cellular_componentsynapse
B0051930biological_processregulation of sensory perception of pain
B0070062cellular_componentextracellular exosome
B0099178biological_processregulation of retrograde trans-synaptic signaling by endocanabinoid
B0120162biological_processpositive regulation of cold-induced thermogenesis
B1990379biological_processlipid transport across blood-brain barrier
C0001972molecular_functionretinoic acid binding
C0005324molecular_functionlong-chain fatty acid transmembrane transporter activity
C0005504molecular_functionfatty acid binding
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0005615cellular_componentextracellular space
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0005886cellular_componentplasma membrane
C0006006biological_processglucose metabolic process
C0006629biological_processlipid metabolic process
C0006656biological_processphosphatidylcholine biosynthetic process
C0006869biological_processlipid transport
C0008289molecular_functionlipid binding
C0008544biological_processepidermis development
C0010829biological_processnegative regulation of glucose transmembrane transport
C0014069cellular_componentpostsynaptic density
C0015908biological_processfatty acid transport
C0015909biological_processlong-chain fatty acid transport
C0030667cellular_componentsecretory granule membrane
C0031392biological_processregulation of prostaglandin biosynthetic process
C0035360biological_processpositive regulation of peroxisome proliferator activated receptor signaling pathway
C0035578cellular_componentazurophil granule lumen
C0042593biological_processglucose homeostasis
C0042802molecular_functionidentical protein binding
C0045202cellular_componentsynapse
C0051930biological_processregulation of sensory perception of pain
C0070062cellular_componentextracellular exosome
C0099178biological_processregulation of retrograde trans-synaptic signaling by endocanabinoid
C0120162biological_processpositive regulation of cold-induced thermogenesis
C1990379biological_processlipid transport across blood-brain barrier
Functional Information from PROSITE/UniProt
site_idPS00214
Number of Residues18
DetailsFABP Cytosolic fatty-acid binding proteins signature. GRWrLvdSkGFDeYMKEL
ChainResidueDetails
AGLY9-LEU26

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues9
DetailsBINDING: BINDING => ECO:0000269|PubMed:24531463, ECO:0007744|PDB:4AZR
ChainResidueDetails
ACYS43
AARG109
ATYR131
BCYS43
BARG109
BTYR131
CCYS43
CARG109
CTYR131

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:24692551, ECO:0007744|PDB:4LKT
ChainResidueDetails
AARG129
BARG129
CARG129

site_idSWS_FT_FI3
Number of Residues3
DetailsMOD_RES: N-acetylalanine => ECO:0000269|PubMed:12665801, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712
ChainResidueDetails
AALA2
BALA2
CALA2

site_idSWS_FT_FI4
Number of Residues3
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS17
BLYS17
CLYS17

site_idSWS_FT_FI5
Number of Residues3
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455
ChainResidueDetails
ATYR131
BTYR131
CTYR131

222415

PDB entries from 2024-07-10

PDB statisticsPDBj update infoContact PDBjnumon