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4LKP

Crystal Structure of Apo Human Epidermal Fatty Acid Binding Protein (FABP5)

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
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 201
ChainResidue
ALYS110
ALYS112

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE DMS A 202
ChainResidue
ALYS24
ATHR46
AASP48
ALEU52
ATHR53
AHOH316
AHOH356

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE DMS A 203
ChainResidue
ALYS72
APHE73
AGLU74
ATHR108
AGLU119
AVAL121
AHOH346

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NH4 A 204
ChainResidue
ALYS17
AGLY18
ASO4205

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 205
ChainResidue
ASER16
ALYS17
AGLY18
APHE19
AASP20
ANH4204
AHOH340
AHOH375

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 Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:24531463, ECO:0007744|PDB:4AZR
ChainResidueDetails
ATYR131
ACYS43
AARG109

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:24692551, ECO:0007744|PDB:4LKT
ChainResidueDetails
AARG129

site_idSWS_FT_FI3
Number of Residues1
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

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS17

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455
ChainResidueDetails
ATYR131

221051

PDB entries from 2024-06-12

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