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3WXQ

Serial femtosecond X-ray structure of human fatty acid-binding protein type-3 (FABP3) in complex with stearic acid (C18:0) determined using X-ray free-electron laser at SACLA

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005615cellular_componentextracellular space
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008092molecular_functioncytoskeletal protein binding
A0008285biological_processnegative regulation of cell population proliferation
A0008289molecular_functionlipid binding
A0015909biological_processlong-chain fatty acid transport
A0032365biological_processintracellular lipid transport
A0036041molecular_functionlong-chain fatty acid binding
A0042632biological_processcholesterol homeostasis
A0046320biological_processregulation of fatty acid oxidation
A0050873biological_processbrown fat cell differentiation
A0055091biological_processphospholipid homeostasis
A0070062cellular_componentextracellular exosome
A0070538molecular_functionoleic acid binding
A0071073biological_processpositive regulation of phospholipid biosynthetic process
A0140214biological_processpositive regulation of long-chain fatty acid import into cell
A2001245biological_processregulation of phosphatidylcholine biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE STE A 200
ChainResidue
ATHR54
ALYS59
AARG79
ALEU116
AARG127
ATYR129
AHOH337
AHOH367

Functional Information from PROSITE/UniProt
site_idPS00214
Number of Residues18
DetailsFABP Cytosolic fatty-acid binding proteins signature. GTWkLvdSkNFDdYMKSL
ChainResidueDetails
AGLY7-LEU24

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:7922029, ECO:0007744|PDB:1HMT
ChainResidueDetails
AARG127

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N-acetylvaline => ECO:0007744|PubMed:22223895
ChainResidueDetails
AVAL2

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P07483
ChainResidueDetails
ATHR8
ATHR30

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by Tyr-kinases => ECO:0000250|UniProtKB:P07483
ChainResidueDetails
ATYR20

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P07483
ChainResidueDetails
ASER23
ASER83

218853

PDB entries from 2024-04-24

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