6VJR
Oxygen tolerant Archeal 4hydroxybutyrylCoA dehydratase (4HBD) from N. maritimus
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050393 | molecular_function | vinylacetyl-CoA delta-isomerase activity |
| A | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050393 | molecular_function | vinylacetyl-CoA delta-isomerase activity |
| B | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| C | 0016853 | molecular_function | isomerase activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0050393 | molecular_function | vinylacetyl-CoA delta-isomerase activity |
| C | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| D | 0016853 | molecular_function | isomerase activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0050393 | molecular_function | vinylacetyl-CoA delta-isomerase activity |
| D | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | binding site for residue SF4 A 601 |
| Chain | Residue |
| A | CYS103 |
| A | GLU449 |
| A | FE607 |
| A | HOH724 |
| A | HOH761 |
| A | HOH1042 |
| A | HOH1081 |
| A | PHE104 |
| A | CYS107 |
| A | VAL108 |
| A | HIS295 |
| A | SER298 |
| A | TYR299 |
| A | CYS301 |
| A | LYS302 |
| site_id | AC2 |
| Number of Residues | 30 |
| Details | binding site for residue FAD A 602 |
| Chain | Residue |
| A | GLY151 |
| A | MET153 |
| A | THR154 |
| A | LYS157 |
| A | ARG160 |
| A | HIS192 |
| A | GLN193 |
| A | THR194 |
| A | GLU260 |
| A | GLU449 |
| A | HIS452 |
| A | SER456 |
| A | PO4606 |
| A | HOH707 |
| A | HOH792 |
| A | HOH803 |
| A | HOH926 |
| A | HOH930 |
| A | HOH934 |
| A | HOH943 |
| A | HOH955 |
| A | HOH1016 |
| C | HIS327 |
| C | ASP388 |
| C | ILE389 |
| C | GLY391 |
| C | GLY392 |
| C | HOH863 |
| C | HOH864 |
| C | HOH872 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 A 603 |
| Chain | Residue |
| A | ILE68 |
| A | GLU81 |
| A | GLY359 |
| A | VAL360 |
| A | HOH708 |
| A | HOH785 |
| A | HOH846 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 604 |
| Chain | Residue |
| A | PHE28 |
| A | HOH718 |
| C | LYS401 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 A 605 |
| Chain | Residue |
| A | LYS401 |
| C | PHE28 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue PO4 A 606 |
| Chain | Residue |
| A | ALA459 |
| A | ILE462 |
| A | FAD602 |
| A | HOH707 |
| A | HOH954 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue FE A 607 |
| Chain | Residue |
| A | HIS295 |
| A | TYR299 |
| A | GLU449 |
| A | SF4601 |
| site_id | AC8 |
| Number of Residues | 12 |
| Details | binding site for residue SF4 B 601 |
| Chain | Residue |
| B | CYS103 |
| B | PHE104 |
| B | CYS107 |
| B | HIS295 |
| B | SER298 |
| B | TYR299 |
| B | CYS301 |
| B | LYS302 |
| B | GLU449 |
| B | FE604 |
| B | HOH904 |
| B | HOH905 |
| site_id | AC9 |
| Number of Residues | 29 |
| Details | binding site for residue FAD B 602 |
| Chain | Residue |
| D | HIS327 |
| D | ASP388 |
| D | ILE389 |
| D | GLY391 |
| D | GLY392 |
| D | HOH854 |
| D | HOH855 |
| D | HOH874 |
| B | GLY151 |
| B | MET153 |
| B | THR154 |
| B | LYS157 |
| B | ARG160 |
| B | HIS192 |
| B | GLN193 |
| B | THR194 |
| B | GLU260 |
| B | GLU449 |
| B | HIS452 |
| B | SER456 |
| B | HOH782 |
| B | HOH800 |
| B | HOH817 |
| B | HOH873 |
| B | HOH909 |
| B | HOH910 |
| B | HOH936 |
| B | HOH972 |
| B | HOH1008 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 B 603 |
| Chain | Residue |
| B | GLU381 |
| B | HOH740 |
| B | HOH976 |
| D | TYR380 |
| D | GLU381 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue FE B 604 |
| Chain | Residue |
| B | HIS295 |
| B | TYR299 |
| B | GLU449 |
| B | SF4601 |
| site_id | AD3 |
| Number of Residues | 12 |
| Details | binding site for residue SF4 C 601 |
| Chain | Residue |
| C | CYS103 |
| C | PHE104 |
| C | CYS107 |
| C | VAL108 |
| C | HIS295 |
| C | TYR299 |
| C | CYS301 |
| C | LYS302 |
| C | GLU449 |
| C | FE603 |
| C | HOH731 |
| C | HOH1033 |
| site_id | AD4 |
| Number of Residues | 29 |
| Details | binding site for residue FAD C 602 |
| Chain | Residue |
| A | HIS327 |
| A | ASP388 |
| A | ILE389 |
| A | GLY391 |
| A | GLY392 |
| A | HOH859 |
| A | HOH863 |
| A | HOH910 |
| C | GLY151 |
| C | MET153 |
| C | THR154 |
| C | LYS157 |
| C | ARG160 |
| C | HIS192 |
| C | GLN193 |
| C | THR194 |
| C | GLU260 |
| C | GLU449 |
| C | HIS452 |
| C | SER456 |
| C | HOH757 |
| C | HOH810 |
| C | HOH831 |
| C | HOH833 |
| C | HOH898 |
| C | HOH904 |
| C | HOH914 |
| C | HOH949 |
| C | HOH1001 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue FE C 603 |
| Chain | Residue |
| C | HIS295 |
| C | TYR299 |
| C | GLU449 |
| C | SF4601 |
| site_id | AD6 |
| Number of Residues | 13 |
| Details | binding site for residue SF4 D 601 |
| Chain | Residue |
| D | CYS103 |
| D | PHE104 |
| D | CYS107 |
| D | VAL108 |
| D | HIS295 |
| D | TYR299 |
| D | CYS301 |
| D | LYS302 |
| D | GLU449 |
| D | FE603 |
| D | HOH849 |
| D | HOH1019 |
| D | HOH1039 |
| site_id | AD7 |
| Number of Residues | 29 |
| Details | binding site for residue FAD D 602 |
| Chain | Residue |
| B | HIS327 |
| B | ASP388 |
| B | ILE389 |
| B | GLY391 |
| B | GLY392 |
| B | HOH841 |
| B | HOH868 |
| B | HOH882 |
| D | GLY151 |
| D | MET153 |
| D | THR154 |
| D | LYS157 |
| D | ARG160 |
| D | HIS192 |
| D | GLN193 |
| D | THR194 |
| D | GLU260 |
| D | GLU449 |
| D | HIS452 |
| D | SER456 |
| D | HOH771 |
| D | HOH780 |
| D | HOH789 |
| D | HOH880 |
| D | HOH915 |
| D | HOH923 |
| D | HOH925 |
| D | HOH957 |
| D | HOH995 |
| site_id | AD8 |
| Number of Residues | 4 |
| Details | binding site for residue FE D 603 |
| Chain | Residue |
| D | HIS295 |
| D | TYR299 |
| D | GLU449 |
| D | SF4601 |
