2HMB
THREE-DIMENSIONAL STRUCTURE OF RECOMBINANT HUMAN MUSCLE FATTY ACID-BINDING PROTEIN
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005615 | cellular_component | extracellular space |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0008092 | molecular_function | cytoskeletal protein binding |
| A | 0008285 | biological_process | negative regulation of cell population proliferation |
| A | 0008289 | molecular_function | lipid binding |
| A | 0015909 | biological_process | long-chain fatty acid transport |
| A | 0032365 | biological_process | intracellular lipid transport |
| A | 0036041 | molecular_function | long-chain fatty acid binding |
| A | 0042632 | biological_process | cholesterol homeostasis |
| A | 0046320 | biological_process | regulation of fatty acid oxidation |
| A | 0050873 | biological_process | brown fat cell differentiation |
| A | 0055091 | biological_process | phospholipid homeostasis |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0070538 | molecular_function | oleic acid binding |
| A | 0071073 | biological_process | positive regulation of phospholipid biosynthetic process |
| A | 0140214 | biological_process | positive regulation of long-chain fatty acid import into cell |
| A | 2001245 | biological_process | regulation of phosphatidylcholine biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PLM A 133 |
| Chain | Residue |
| A | ALA33 |
| A | ARG126 |
| A | TYR128 |
| A | HOH134 |
| A | HOH135 |
Functional Information from PROSITE/UniProt
| site_id | PS00214 |
| Number of Residues | 18 |
| Details | FABP Cytosolic fatty-acid binding proteins signature. GTWkLvdSkNFDdYMKSL |
| Chain | Residue | Details |
| A | GLY6-LEU23 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:7922029, ECO:0007744|PDB:1HMT |
| Chain | Residue | Details |
| A | THR127 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | MOD_RES: N-acetylvaline => ECO:0007744|PubMed:22223895 |
| Chain | Residue | Details |
| A | ASP2 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P07483 |
| Chain | Residue | Details |
| A | TRP8 | |
| A | ARG30 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine; by Tyr-kinases => ECO:0000250|UniProtKB:P07483 |
| Chain | Residue | Details |
| A | MET20 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P07483 |
| Chain | Residue | Details |
| A | LEU23 | |
| A | ILE83 |
