4X28
Crystal structure of the ChsE4-ChsE5 complex from Mycobacterium tuberculosis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006707 | biological_process | cholesterol catabolic process |
| A | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| A | 0033539 | biological_process | fatty acid beta-oxidation using acyl-CoA dehydrogenase |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| A | 0071949 | molecular_function | FAD binding |
| B | 0006707 | biological_process | cholesterol catabolic process |
| B | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| B | 0033539 | biological_process | fatty acid beta-oxidation using acyl-CoA dehydrogenase |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0071949 | molecular_function | FAD binding |
| C | 0006707 | biological_process | cholesterol catabolic process |
| C | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| D | 0006707 | biological_process | cholesterol catabolic process |
| D | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 29 |
| Details | binding site for residue FDA A 501 |
| Chain | Residue |
| A | ILE127 |
| A | GLU382 |
| A | VAL383 |
| A | HOH668 |
| A | HOH680 |
| A | HOH707 |
| A | HOH804 |
| A | HOH821 |
| A | HOH841 |
| A | HOH898 |
| A | HOH899 |
| A | TYR129 |
| C | GLN262 |
| D | ARG251 |
| D | GLN253 |
| D | PHE254 |
| D | ILE258 |
| D | PHE261 |
| D | VAL264 |
| D | HIS327 |
| D | VAL328 |
| D | GLY331 |
| A | SER130 |
| A | GLY135 |
| A | THR136 |
| A | TRP160 |
| A | SER162 |
| A | PHE376 |
| A | THR380 |
| site_id | AC2 |
| Number of Residues | 28 |
| Details | binding site for residue FDA B 501 |
| Chain | Residue |
| B | ILE127 |
| B | TYR129 |
| B | SER130 |
| B | GLY135 |
| B | THR136 |
| B | TRP160 |
| B | SER162 |
| B | PHE376 |
| B | THR380 |
| B | GLU382 |
| B | VAL383 |
| B | HOH659 |
| B | HOH671 |
| B | HOH672 |
| B | HOH680 |
| B | HOH709 |
| B | HOH777 |
| B | HOH812 |
| B | HOH813 |
| C | ARG251 |
| C | GLN253 |
| C | ILE258 |
| C | PHE261 |
| C | VAL264 |
| C | HIS327 |
| C | VAL328 |
| C | GLY331 |
| D | GLN262 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"26161441","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26161441","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4X28","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
