4IRN
Crystal Structure of the Prolyl Acyl Carrier Protein Oxidase AnaB
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003995 | molecular_function | acyl-CoA dehydrogenase 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 | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| C | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
| C | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| D | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
| D | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| E | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
| E | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| E | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| F | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
| F | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| F | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| G | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
| G | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| G | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| H | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
| H | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| H | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE FAD A 400 |
| Chain | Residue |
| A | PHE87 |
| A | THR367 |
| A | GLU369 |
| A | HOH507 |
| A | HOH556 |
| B | HIS270 |
| B | GLN272 |
| B | PHE273 |
| B | ILE277 |
| B | PHE280 |
| B | VAL283 |
| A | HIS125 |
| B | GLU338 |
| B | ILE339 |
| B | GLY341 |
| B | ALA342 |
| D | GLN281 |
| A | ALA127 |
| A | THR128 |
| A | GLY133 |
| A | SER134 |
| A | TYR158 |
| A | THR160 |
| A | PHE363 |
| site_id | AC2 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE FAD B 400 |
| Chain | Residue |
| A | HIS270 |
| A | GLN272 |
| A | PHE273 |
| A | ILE277 |
| A | PHE280 |
| A | VAL283 |
| A | GLU338 |
| A | ILE339 |
| A | GLY341 |
| A | ALA342 |
| A | HOH504 |
| B | PHE87 |
| B | HIS125 |
| B | ALA127 |
| B | THR128 |
| B | GLY133 |
| B | SER134 |
| B | TYR158 |
| B | THR160 |
| B | PHE363 |
| B | THR367 |
| B | GLU369 |
| B | VAL373 |
| B | HOH517 |
| B | HOH556 |
| C | GLN281 |
| site_id | AC3 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE FAD C 400 |
| Chain | Residue |
| B | GLN281 |
| C | PHE87 |
| C | HIS125 |
| C | ALA127 |
| C | THR128 |
| C | GLY133 |
| C | SER134 |
| C | TYR158 |
| C | THR160 |
| C | PHE363 |
| C | THR367 |
| C | GLU369 |
| C | HOH505 |
| C | HOH560 |
| C | HOH569 |
| D | HIS270 |
| D | PHE273 |
| D | ILE277 |
| D | PHE280 |
| D | VAL283 |
| D | GLU338 |
| D | ILE339 |
| D | GLY341 |
| D | ALA342 |
| site_id | AC4 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE FAD D 400 |
| Chain | Residue |
| D | HOH555 |
| D | HOH556 |
| A | GLN281 |
| C | HIS270 |
| C | GLN272 |
| C | PHE273 |
| C | ILE277 |
| C | PHE280 |
| C | VAL283 |
| C | GLU338 |
| C | ILE339 |
| C | GLY341 |
| C | ALA342 |
| C | HOH573 |
| D | PHE87 |
| D | HIS125 |
| D | ALA127 |
| D | THR128 |
| D | GLY133 |
| D | SER134 |
| D | TYR158 |
| D | THR160 |
| D | PHE363 |
| D | THR367 |
| D | GLU369 |
| D | HOH503 |
| D | HOH504 |
| site_id | AC5 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE FAD E 400 |
| Chain | Residue |
| E | PHE87 |
| E | HIS125 |
| E | ALA127 |
| E | THR128 |
| E | GLY133 |
| E | SER134 |
| E | TYR158 |
| E | THR160 |
| E | PHE363 |
| E | THR367 |
| E | GLU369 |
| F | HIS270 |
| F | GLN272 |
| F | PHE273 |
| F | ILE277 |
| F | PHE280 |
| F | VAL283 |
| F | GLU338 |
| F | ILE339 |
| F | GLY341 |
| F | ALA342 |
| F | HOH541 |
| H | GLN281 |
| site_id | AC6 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE FAD F 400 |
| Chain | Residue |
| E | HIS270 |
| E | GLN272 |
| E | PHE273 |
| E | ILE277 |
| E | PHE280 |
| E | VAL283 |
| E | GLU338 |
| E | ILE339 |
| E | GLY341 |
| E | ALA342 |
| E | HOH534 |
| F | PHE87 |
| F | HIS125 |
| F | ALA127 |
| F | THR128 |
| F | GLY133 |
| F | SER134 |
| F | TYR158 |
| F | THR160 |
| F | PHE363 |
| F | THR367 |
| F | GLU369 |
| F | VAL373 |
| F | HOH538 |
| F | HOH547 |
| G | GLN281 |
| site_id | AC7 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE FAD G 400 |
| Chain | Residue |
| F | GLN281 |
| G | PHE87 |
| G | HIS125 |
| G | ALA127 |
| G | THR128 |
| G | GLY133 |
| G | SER134 |
| G | TYR158 |
| G | THR160 |
| G | PHE363 |
| G | THR367 |
| G | GLU369 |
| G | HOH503 |
| G | HOH544 |
| H | HIS270 |
| H | GLN272 |
| H | PHE273 |
| H | ILE277 |
| H | PHE280 |
| H | VAL283 |
| H | GLU338 |
| H | ILE339 |
| H | GLY341 |
| H | ALA342 |
| site_id | AC8 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE FAD H 400 |
| Chain | Residue |
| E | GLN281 |
| G | HIS270 |
| G | GLN272 |
| G | PHE273 |
| G | ILE277 |
| G | PHE280 |
| G | VAL283 |
| G | GLU338 |
| G | ILE339 |
| G | GLY341 |
| G | ALA342 |
| H | PHE87 |
| H | HIS125 |
| H | ALA127 |
| H | THR128 |
| H | GLY133 |
| H | SER134 |
| H | TYR158 |
| H | THR160 |
| H | PHE363 |
| H | THR367 |
| H | GLU369 |
| H | HOH542 |
