2OR0
Structural Genomics, the crystal structure of a putative hydroxylase from Rhodococcus sp. RHA1
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| A | 0016712 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen |
| A | 0033539 | biological_process | fatty acid beta-oxidation using acyl-CoA dehydrogenase |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0003995 | molecular_function | acyl-CoA dehydrogenase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| B | 0016712 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen |
| B | 0033539 | biological_process | fatty acid beta-oxidation using acyl-CoA dehydrogenase |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT A 601 |
| Chain | Residue |
| A | ASN205 |
| A | ARG213 |
| A | HOH821 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT B 602 |
| Chain | Residue |
| B | PRO159 |
| B | ASN205 |
| B | ARG213 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ACT B 603 |
| Chain | Residue |
| B | ARG313 |
| B | ARG388 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT A 604 |
| Chain | Residue |
| A | HOH865 |
| A | HOH886 |
| A | ARG259 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT B 605 |
| Chain | Residue |
| A | GLY129 |
| B | ASN104 |
| B | ASP105 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT B 606 |
| Chain | Residue |
| B | ARG37 |
| B | ASP105 |
| B | TRP107 |
| B | HIS139 |
| B | HOH762 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT A 607 |
| Chain | Residue |
| A | ASP211 |
| A | PHE310 |
| A | ARG313 |
| A | ARG388 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT B 608 |
| Chain | Residue |
| A | GLU279 |
| A | HOH670 |
| B | ARG329 |
| B | PRO367 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT B 609 |
| Chain | Residue |
| B | GLY2 |
| B | VAL4 |
| B | GLU59 |
| B | HOH878 |
| site_id | BC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ACT A 610 |
| Chain | Residue |
| A | VAL366 |
| A | PRO367 |
| A | GLY368 |
| A | PRO369 |
| A | HOH883 |
| B | TYR272 |
| B | VAL273 |
| B | ARG337 |
| B | HOH883 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ACT A 611 |
| Chain | Residue |
| A | TRP325 |
| A | ARG329 |
| A | ASP332 |
| A | HIS357 |
| A | LEU360 |
| B | GLU333 |
| B | ALA336 |
| site_id | BC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE ACT A 612 |
| Chain | Residue |
| A | ARG213 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| A | PHE225 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| B | PHE225 |
