3P4T
Crystal structure of a putative acyl-CoA dehydrogenase from Mycobacterium smegmatis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
| A | 0006552 | biological_process | L-leucine catabolic process |
| A | 0008470 | molecular_function | isovaleryl-CoA dehydrogenase activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
| B | 0006552 | biological_process | L-leucine catabolic process |
| B | 0008470 | molecular_function | isovaleryl-CoA dehydrogenase activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE FAO B 500 |
| Chain | Residue |
| A | ARG289 |
| B | LEU145 |
| B | ILE147 |
| B | THR148 |
| B | GLY152 |
| B | GLY153 |
| B | SER154 |
| B | TYR178 |
| B | ILE179 |
| B | THR180 |
| B | LYS222 |
| A | THR291 |
| B | ILE380 |
| B | ILE383 |
| B | THR387 |
| B | GLU389 |
| B | HOH411 |
| B | HOH416 |
| B | HOH430 |
| B | HOH434 |
| B | HOH454 |
| B | HOH514 |
| A | LEU296 |
| B | HOH610 |
| B | HOH673 |
| A | ARG299 |
| A | GLN300 |
| A | GLN358 |
| A | LEU359 |
| A | GLY361 |
| A | GLY362 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 501 |
| Chain | Residue |
| A | GLN276 |
| A | ALA310 |
| A | ARG317 |
| A | HOH408 |
| A | HOH786 |
| B | LEU399 |
| site_id | AC3 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE FAO A 500 |
| Chain | Residue |
| A | LEU145 |
| A | ILE147 |
| A | THR148 |
| A | GLY152 |
| A | GLY153 |
| A | SER154 |
| A | TYR178 |
| A | ILE179 |
| A | THR180 |
| A | LYS222 |
| A | ILE380 |
| A | ILE383 |
| A | THR387 |
| A | GLU389 |
| A | HOH416 |
| A | HOH463 |
| A | HOH530 |
| A | HOH575 |
| A | HOH590 |
| A | HOH608 |
| A | HOH618 |
| A | HOH686 |
| B | ARG289 |
| B | THR291 |
| B | LEU296 |
| B | ARG299 |
| B | GLN300 |
| B | GLN358 |
| B | LEU359 |
| B | GLY361 |
| B | GLY362 |
| B | HOH490 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 501 |
| Chain | Residue |
| A | LEU399 |
| B | GLN276 |
| B | ALA310 |
| B | ARG317 |
| B | HOH842 |
| B | HOH843 |
Functional Information from PROSITE/UniProt
| site_id | PS00073 |
| Number of Residues | 20 |
| Details | ACYL_COA_DH_2 Acyl-CoA dehydrogenases signature 2. QlFGGmGYmaEseveRqyrD |
| Chain | Residue | Details |
| A | GLN358-ASP377 |
