5D4A
Crystal Structure of FABP4 in complex with 3-(2-phenyl-1H-indol-1-yl)propanoic acid
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005324 | molecular_function | long-chain fatty acid transmembrane transporter activity |
| A | 0005504 | molecular_function | fatty acid binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005811 | cellular_component | lipid droplet |
| A | 0005829 | cellular_component | cytosol |
| A | 0008289 | molecular_function | lipid binding |
| A | 0009617 | biological_process | response to bacterium |
| A | 0015908 | biological_process | fatty acid transport |
| A | 0015909 | biological_process | long-chain fatty acid transport |
| A | 0036041 | molecular_function | long-chain fatty acid binding |
| A | 0042632 | biological_process | cholesterol homeostasis |
| A | 0045892 | biological_process | negative regulation of DNA-templated transcription |
| A | 0050729 | biological_process | positive regulation of inflammatory response |
| A | 0050872 | biological_process | white fat cell differentiation |
| A | 0050873 | biological_process | brown fat cell differentiation |
| A | 0051427 | molecular_function | hormone receptor binding |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0071285 | biological_process | cellular response to lithium ion |
| A | 0071356 | biological_process | cellular response to tumor necrosis factor |
| A | 0120162 | biological_process | positive regulation of cold-induced thermogenesis |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | binding site for residue 57Q A 201 |
| Chain | Residue |
| A | PHE16 |
| A | HOH344 |
| A | TYR19 |
| A | PRO38 |
| A | PHE57 |
| A | ASP76 |
| A | ARG78 |
| A | ARG126 |
| A | TYR128 |
| A | HOH326 |
Functional Information from PROSITE/UniProt
| site_id | PS00214 |
| Number of Residues | 18 |
| Details | FABP Cytosolic fatty-acid binding proteins signature. GTWkLvsSeNFDdYMKEV |
| Chain | Residue | Details |
| A | GLY6-VAL23 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ARG126 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | MOD_RES: N-acetylcysteine => ECO:0007744|PubMed:22223895 |
| Chain | Residue | Details |
| A | CYS1 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P04117 |
| Chain | Residue | Details |
| A | SER12 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine; by Tyr-kinases => ECO:0000250 |
| Chain | Residue | Details |
| A | TYR19 |
