3R9B
Crystal structure of Mycobacterium smegmatis CYP164A2 in ligand free state
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0008202 | biological_process | steroid metabolic process |
| A | 0008203 | biological_process | cholesterol metabolic process |
| A | 0016042 | biological_process | lipid catabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| A | 0020037 | molecular_function | heme binding |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0008202 | biological_process | steroid metabolic process |
| B | 0008203 | biological_process | cholesterol metabolic process |
| B | 0016042 | biological_process | lipid catabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| B | 0020037 | molecular_function | heme binding |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0004497 | molecular_function | monooxygenase activity |
| C | 0005506 | molecular_function | iron ion binding |
| C | 0006629 | biological_process | lipid metabolic process |
| C | 0008202 | biological_process | steroid metabolic process |
| C | 0008203 | biological_process | cholesterol metabolic process |
| C | 0016042 | biological_process | lipid catabolic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| C | 0020037 | molecular_function | heme binding |
| C | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE HEM A 501 |
| Chain | Residue |
| A | PHE97 |
| A | LEU264 |
| A | MET297 |
| A | VAL303 |
| A | ARG308 |
| A | GLY358 |
| A | PHE359 |
| A | GLY360 |
| A | ALA363 |
| A | HIS364 |
| A | CYS366 |
| A | LEU98 |
| A | GLY368 |
| A | ALA372 |
| A | D12509 |
| A | HOH615 |
| A | HOH696 |
| A | HIS105 |
| A | ARG109 |
| A | ILE159 |
| A | LEU252 |
| A | LEU253 |
| A | ALA256 |
| A | THR260 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 A 502 |
| Chain | Residue |
| A | GLU235 |
| A | THR242 |
| A | GLU243 |
| A | K507 |
| A | HOH707 |
| A | HOH828 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 A 503 |
| Chain | Residue |
| A | ARG109 |
| A | SER113 |
| A | NA506 |
| A | HOH744 |
| A | HOH834 |
| B | ASN50 |
| B | ARG81 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 504 |
| Chain | Residue |
| A | VAL341 |
| A | GLY342 |
| A | ARG351 |
| A | GLN353 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 505 |
| Chain | Residue |
| A | ILE78 |
| A | TYR309 |
| A | THR326 |
| A | HOH753 |
| A | HOH775 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA A 506 |
| Chain | Residue |
| A | GLY110 |
| A | SER113 |
| A | PO4503 |
| A | HOH835 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K A 507 |
| Chain | Residue |
| A | GLU235 |
| A | GLY238 |
| A | LEU241 |
| A | PO4502 |
| A | HOH785 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 508 |
| Chain | Residue |
| A | ARG109 |
| A | GLY362 |
| A | ALA363 |
| A | HOH835 |
| B | PRO47 |
| B | GLU48 |
| B | ARG81 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE D12 A 509 |
| Chain | Residue |
| A | LEU252 |
| A | ALA256 |
| A | HEM501 |
| site_id | BC1 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE HEM B 501 |
| Chain | Residue |
| B | PHE97 |
| B | LEU98 |
| B | HIS105 |
| B | ARG109 |
| B | ILE159 |
| B | LEU252 |
| B | LEU253 |
| B | ALA256 |
| B | THR260 |
| B | THR261 |
| B | LEU264 |
| B | MET297 |
| B | VAL303 |
| B | ARG308 |
| B | GLY358 |
| B | PHE359 |
| B | GLY360 |
| B | ALA363 |
| B | HIS364 |
| B | CYS366 |
| B | GLY368 |
| B | ALA372 |
| B | D12509 |
| B | HOH668 |
| B | HOH669 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 B 502 |
| Chain | Residue |
| B | GLU235 |
| B | THR242 |
| B | GLU243 |
| B | K508 |
| B | HOH741 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 503 |
| Chain | Residue |
| B | EDO506 |
| B | VAL341 |
| B | GLY342 |
| B | ARG351 |
| B | GLN353 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 504 |
| Chain | Residue |
| B | SER76 |
| B | ILE78 |
| B | TYR309 |
| B | THR326 |
| B | HOH646 |
| B | HOH822 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 505 |
| Chain | Residue |
| B | ALA343 |
| B | ARG346 |
| C | ASP350 |
| C | ARG351 |
| C | ALA352 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 506 |
| Chain | Residue |
| B | GLY342 |
| B | ARG346 |
| B | ASP348 |
| B | ARG351 |
| B | EDO503 |
| site_id | BC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 507 |
| Chain | Residue |
| B | SER56 |
| B | ASP59 |
| B | GLY317 |
| B | HOH647 |
| site_id | BC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE K B 508 |
| Chain | Residue |
| B | GLU235 |
| B | GLY238 |
| B | LEU241 |
| B | PO4502 |
| site_id | BC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE D12 B 509 |
| Chain | Residue |
| B | LEU98 |
| B | LEU184 |
| B | ASN251 |
| B | HEM501 |
| site_id | CC1 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE HEM C 501 |
| Chain | Residue |
| C | PHE97 |
| C | LEU98 |
| C | HIS105 |
| C | ARG109 |
| C | ILE159 |
| C | LEU252 |
| C | LEU253 |
| C | ALA256 |
| C | THR260 |
| C | THR261 |
| C | LEU264 |
| C | MET297 |
| C | VAL303 |
| C | ARG308 |
| C | GLY358 |
| C | PHE359 |
| C | GLY360 |
| C | HIS364 |
| C | CYS366 |
| C | GLY368 |
| C | ALA372 |
| C | D12513 |
| C | HOH642 |
| C | HOH654 |
| site_id | CC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 C 502 |
| Chain | Residue |
| C | GLU235 |
| C | THR242 |
| C | GLU243 |
| C | K512 |
| C | HOH687 |
| site_id | CC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 C 503 |
| Chain | Residue |
| B | ARG109 |
| B | SER113 |
| C | ASN50 |
| C | ARG81 |
| C | NA511 |
| C | HOH614 |
| C | HOH772 |
| site_id | CC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO C 504 |
| Chain | Residue |
| C | ALA183 |
| C | ASP185 |
| C | PHE187 |
| C | LEU188 |
| C | HOH627 |
| C | HOH656 |
| C | HOH727 |
| C | HOH757 |
| site_id | CC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO C 505 |
| Chain | Residue |
| A | PRO47 |
| A | GLU48 |
| A | ARG81 |
| C | ARG109 |
| C | GLY362 |
| C | ALA363 |
| C | EDO508 |
| C | HOH779 |
| site_id | CC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO C 506 |
| Chain | Residue |
| C | VAL341 |
| C | GLY342 |
| C | ARG351 |
| C | GLN353 |
| site_id | CC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO C 507 |
| Chain | Residue |
| B | ARG109 |
| B | ALA363 |
| B | HOH602 |
| C | PRO47 |
| C | GLU48 |
| C | ARG81 |
| site_id | CC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO C 508 |
| Chain | Residue |
| C | ARG109 |
| C | GLY110 |
| C | SER113 |
| C | EDO505 |
| C | HOH779 |
| C | HOH819 |
| site_id | CC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO C 509 |
| Chain | Residue |
| C | SER76 |
| C | PHE79 |
| C | TYR309 |
| C | THR326 |
| C | HOH727 |
| C | HOH790 |
| site_id | DC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO C 510 |
| Chain | Residue |
| C | SER56 |
| C | ASP59 |
| C | GLY317 |
| C | HOH641 |
| site_id | DC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA C 511 |
| Chain | Residue |
| B | GLY110 |
| B | SER113 |
| B | HOH602 |
| C | PO4503 |
| C | HOH825 |
| site_id | DC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K C 512 |
| Chain | Residue |
| C | GLU235 |
| C | GLY238 |
| C | LEU241 |
| C | PO4502 |
| C | HOH648 |
| site_id | DC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE D12 C 513 |
| Chain | Residue |
| C | LEU184 |
| C | LEU252 |
| C | ILE255 |
| C | ALA256 |
| C | HEM501 |
Functional Information from PROSITE/UniProt
| site_id | PS00086 |
| Number of Residues | 10 |
| Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGkGAHFCLG |
| Chain | Residue | Details |
| A | PHE359-GLY368 |
