Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005504 | molecular_function | fatty acid binding |
A | 0005515 | molecular_function | protein binding |
A | 0005634 | cellular_component | nucleus |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0008289 | molecular_function | lipid binding |
A | 0015485 | molecular_function | cholesterol binding |
A | 0015908 | biological_process | fatty acid transport |
A | 0043209 | cellular_component | myelin sheath |
A | 0061024 | biological_process | membrane organization |
A | 0070062 | cellular_component | extracellular exosome |
B | 0005504 | molecular_function | fatty acid binding |
B | 0005515 | molecular_function | protein binding |
B | 0005634 | cellular_component | nucleus |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0008289 | molecular_function | lipid binding |
B | 0015485 | molecular_function | cholesterol binding |
B | 0015908 | biological_process | fatty acid transport |
B | 0043209 | cellular_component | myelin sheath |
B | 0061024 | biological_process | membrane organization |
B | 0070062 | cellular_component | extracellular exosome |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | binding site for residue PLM A 201 |
Chain | Residue |
A | THR30 |
A | PRO39 |
A | SER56 |
A | ASP77 |
A | ARG107 |
A | ARG127 |
A | TYR129 |
site_id | AC2 |
Number of Residues | 7 |
Details | binding site for residue PLM B 201 |
Chain | Residue |
B | PHE58 |
B | ARG107 |
B | ARG127 |
B | TYR129 |
B | HOH302 |
B | LEU24 |
B | SER56 |
Functional Information from PROSITE/UniProt
site_id | PS00214 |
Number of Residues | 18 |
Details | FABP Cytosolic fatty-acid binding proteins signature. GTWkLvsSeNFDdYMKAL |
Chain | Residue | Details |
A | GLY7-LEU24 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ARG107 | |
A | ARG127 | |
B | ARG107 | |
B | ARG127 | |
Chain | Residue | Details |
A | SER2 | |
B | SER2 | |