3R7K
Crystal structure of a probable acyl CoA dehydrogenase from Mycobacterium abscessus ATCC 19977 / DSM 44196
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| 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 | 0046359 | biological_process | butyrate catabolic process |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| 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 | 0046359 | biological_process | butyrate catabolic process |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| C | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| C | 0033539 | biological_process | fatty acid beta-oxidation using acyl-CoA dehydrogenase |
| C | 0046359 | biological_process | butyrate catabolic process |
| C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| D | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| D | 0033539 | biological_process | fatty acid beta-oxidation using acyl-CoA dehydrogenase |
| D | 0046359 | biological_process | butyrate catabolic process |
| D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE FDA A 420 |
| Chain | Residue |
| A | ILE114 |
| A | ILE378 |
| A | ILE381 |
| A | THR385 |
| A | GLU387 |
| A | GLU391 |
| A | HOH415 |
| B | ARG288 |
| B | THR290 |
| B | PHE291 |
| B | LEU295 |
| A | LEU144 |
| B | ARG298 |
| B | ILE300 |
| B | GLN356 |
| B | ILE357 |
| B | GLY360 |
| C | GLN299 |
| A | VAL146 |
| A | THR147 |
| A | GLY152 |
| A | SER153 |
| A | PHE177 |
| A | ILE178 |
| A | THR179 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE K A 400 |
| Chain | Residue |
| A | THR93 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE K A 401 |
| Chain | Residue |
| A | TYR373 |
| A | HOH416 |
| B | TYR373 |
| B | HOH408 |
| site_id | AC4 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE FDA B 420 |
| Chain | Residue |
| A | ARG288 |
| A | THR290 |
| A | PHE291 |
| A | LEU295 |
| A | ARG298 |
| A | ILE301 |
| A | GLN356 |
| A | ILE357 |
| A | GLY359 |
| A | GLY360 |
| B | LEU144 |
| B | VAL146 |
| B | THR147 |
| B | GLY152 |
| B | SER153 |
| B | PHE177 |
| B | ILE178 |
| B | THR179 |
| B | LYS221 |
| B | ILE381 |
| B | THR385 |
| B | GLU387 |
| D | GLN299 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE K B 400 |
| Chain | Residue |
| B | SER89 |
| B | THR93 |
| site_id | AC6 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE FDA C 420 |
| Chain | Residue |
| A | GLN299 |
| C | ILE114 |
| C | LEU144 |
| C | VAL146 |
| C | THR147 |
| C | GLY152 |
| C | SER153 |
| C | PHE177 |
| C | ILE178 |
| C | THR179 |
| C | ILE378 |
| C | ILE381 |
| C | THR385 |
| C | GLU387 |
| D | ARG288 |
| D | THR290 |
| D | LEU295 |
| D | ILE301 |
| D | GLN356 |
| D | ILE357 |
| D | GLY360 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE K C 400 |
| Chain | Residue |
| C | SER89 |
| C | THR93 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K C 401 |
| Chain | Residue |
| C | TYR373 |
| C | HOH412 |
| C | HOH413 |
| C | HOH414 |
| D | TYR373 |
| D | HOH412 |
| site_id | AC9 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE FDA D 420 |
| Chain | Residue |
| D | PHE177 |
| D | ILE178 |
| D | THR179 |
| D | LYS221 |
| D | ILE381 |
| D | THR385 |
| D | GLU387 |
| B | GLN299 |
| C | ARG288 |
| C | THR290 |
| C | PHE291 |
| C | LEU295 |
| C | ARG298 |
| C | ILE301 |
| C | GLN356 |
| C | ILE357 |
| C | GLY360 |
| D | LEU144 |
| D | VAL146 |
| D | THR147 |
| D | GLY152 |
| D | SER153 |
| site_id | BC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE K D 400 |
| Chain | Residue |
| D | THR93 |
Functional Information from PROSITE/UniProt
| site_id | PS00073 |
| Number of Residues | 20 |
| Details | ACYL_COA_DH_2 Acyl-CoA dehydrogenases signature 2. QiFGGmGYmrEseieRhyrD |
| Chain | Residue | Details |
| A | GLN356-ASP375 |
