4EGN
The X-ray crystal structure of CYP199A4 in complex with veratric acid
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004497 | molecular_function | monooxygenase activity |
A | 0005506 | molecular_function | iron ion binding |
A | 0006707 | biological_process | cholesterol catabolic process |
A | 0008395 | molecular_function | steroid hydroxylase 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 | 0036199 | molecular_function | cholest-4-en-3-one 26-monooxygenase activity |
A | 0046872 | molecular_function | metal ion binding |
B | 0004497 | molecular_function | monooxygenase activity |
B | 0005506 | molecular_function | iron ion binding |
B | 0006707 | biological_process | cholesterol catabolic process |
B | 0008395 | molecular_function | steroid hydroxylase 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 | 0036199 | molecular_function | cholest-4-en-3-one 26-monooxygenase activity |
B | 0046872 | molecular_function | metal ion binding |
C | 0004497 | molecular_function | monooxygenase activity |
C | 0005506 | molecular_function | iron ion binding |
C | 0006707 | biological_process | cholesterol catabolic process |
C | 0008395 | molecular_function | steroid hydroxylase 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 | 0036199 | molecular_function | cholest-4-en-3-one 26-monooxygenase activity |
C | 0046872 | molecular_function | metal ion binding |
D | 0004497 | molecular_function | monooxygenase activity |
D | 0005506 | molecular_function | iron ion binding |
D | 0006707 | biological_process | cholesterol catabolic process |
D | 0008395 | molecular_function | steroid hydroxylase activity |
D | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
D | 0020037 | molecular_function | heme binding |
D | 0036199 | molecular_function | cholest-4-en-3-one 26-monooxygenase activity |
D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE HEM A 501 |
Chain | Residue |
A | ILE97 |
A | PHE298 |
A | ARG300 |
A | GLY350 |
A | PHE351 |
A | GLY352 |
A | HIS356 |
A | CYS358 |
A | VAL359 |
A | GLY360 |
A | TWO504 |
A | LEU98 |
A | HOH615 |
A | HOH622 |
A | HIS105 |
A | ARG109 |
A | PHE160 |
A | ALA248 |
A | GLY249 |
A | THR252 |
A | THR253 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 502 |
Chain | Residue |
A | ARG109 |
A | SER113 |
A | GOL503 |
A | HOH824 |
D | LYS114 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 503 |
Chain | Residue |
A | SER113 |
A | LEU116 |
A | SER117 |
A | VAL359 |
A | GLN361 |
A | SO4502 |
A | HOH748 |
site_id | AC4 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE TWO A 504 |
Chain | Residue |
A | ARG92 |
A | SER95 |
A | ILE97 |
A | LEU98 |
A | VAL181 |
A | PHE182 |
A | PHE185 |
A | SER244 |
A | SER247 |
A | ALA248 |
A | HEM501 |
A | HOH652 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL A 505 |
Chain | Residue |
A | ARG92 |
A | TYR177 |
A | GLN203 |
site_id | AC6 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE HEM B 501 |
Chain | Residue |
B | ILE97 |
B | LEU98 |
B | HIS105 |
B | ARG109 |
B | PHE160 |
B | ALA248 |
B | GLY249 |
B | THR252 |
B | THR253 |
B | PHE298 |
B | ARG300 |
B | GLY350 |
B | PHE351 |
B | GLY352 |
B | HIS356 |
B | CYS358 |
B | VAL359 |
B | GLY360 |
B | TWO505 |
B | HOH607 |
B | HOH644 |
site_id | AC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 B 502 |
Chain | Residue |
B | ARG109 |
B | SER113 |
B | GOL504 |
B | HOH670 |
B | HOH779 |
B | HOH880 |
B | HOH903 |
C | LYS114 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL B 503 |
Chain | Residue |
B | SER334 |
B | ASP335 |
B | LEU338 |
B | ASP340 |
B | ARG343 |
site_id | AC9 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL B 504 |
Chain | Residue |
B | SER113 |
B | LEU116 |
B | SER117 |
B | GLN361 |
B | LEU362 |
B | SO4502 |
B | HOH793 |
B | HOH838 |
site_id | BC1 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE TWO B 505 |
Chain | Residue |
B | ALA248 |
B | HEM501 |
B | HOH666 |
B | ARG92 |
B | SER95 |
B | ILE97 |
B | LEU98 |
B | VAL181 |
B | PHE182 |
B | PHE185 |
B | SER244 |
B | SER247 |
site_id | BC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL B 506 |
Chain | Residue |
B | ARG92 |
B | TYR177 |
B | GLN203 |
B | HOH698 |
site_id | BC3 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE HEM C 501 |
Chain | Residue |
C | ILE97 |
C | LEU98 |
C | HIS105 |
C | ARG109 |
C | ALA248 |
C | GLY249 |
C | THR252 |
C | THR253 |
C | VAL295 |
C | PHE298 |
C | ARG300 |
C | LEU323 |
C | GLY350 |
C | PHE351 |
C | GLY352 |
C | HIS356 |
C | CYS358 |
C | VAL359 |
C | GLY360 |
C | ALA364 |
C | TWO506 |
C | HOH609 |
C | HOH628 |
site_id | BC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 C 502 |
Chain | Residue |
B | LYS114 |
C | ARG109 |
C | SER113 |
C | GOL505 |
C | HOH649 |
C | HOH663 |
C | HOH830 |
C | HOH881 |
site_id | BC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 C 503 |
Chain | Residue |
B | ARG107 |
B | HOH729 |
B | HOH743 |
C | ARG107 |
C | HOH653 |
C | HOH832 |
site_id | BC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 C 504 |
Chain | Residue |
C | ARG60 |
C | HOH718 |
C | HOH773 |
C | HOH934 |
site_id | BC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL C 505 |
Chain | Residue |
C | SER113 |
C | LEU116 |
C | SER117 |
C | VAL359 |
C | GLN361 |
C | SO4502 |
C | HOH839 |
site_id | BC8 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE TWO C 506 |
Chain | Residue |
C | ARG92 |
C | SER95 |
C | LEU98 |
C | VAL181 |
C | PHE182 |
C | PHE185 |
C | SER244 |
C | SER247 |
C | ALA248 |
C | PHE298 |
C | HEM501 |
C | HOH644 |
site_id | BC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL C 507 |
Chain | Residue |
C | ARG92 |
C | TYR177 |
C | GLN203 |
C | HOH796 |
site_id | CC1 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE HEM D 501 |
Chain | Residue |
D | ILE97 |
D | LEU98 |
D | HIS105 |
D | ARG109 |
D | LEU116 |
D | PHE160 |
D | ALA248 |
D | GLY249 |
D | THR252 |
D | THR253 |
D | VAL295 |
D | PHE298 |
D | ARG300 |
D | LEU323 |
D | GLY350 |
D | PHE351 |
D | GLY352 |
D | HIS356 |
D | CYS358 |
D | VAL359 |
D | GLY360 |
D | ALA364 |
D | TWO506 |
D | HOH607 |
D | HOH622 |
site_id | CC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 D 502 |
Chain | Residue |
D | ARG109 |
D | SER113 |
D | GOL505 |
D | HOH856 |
site_id | CC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 D 503 |
Chain | Residue |
A | ARG107 |
A | HOH692 |
D | ARG107 |
D | HOH703 |
D | HOH799 |
site_id | CC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 D 504 |
Chain | Residue |
D | ARG60 |
D | HOH682 |
site_id | CC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL D 505 |
Chain | Residue |
D | SER113 |
D | LEU116 |
D | SER117 |
D | VAL359 |
D | GLN361 |
D | SO4502 |
D | HOH824 |
site_id | CC6 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE TWO D 506 |
Chain | Residue |
D | ARG92 |
D | SER95 |
D | ILE97 |
D | LEU98 |
D | VAL181 |
D | PHE182 |
D | PHE185 |
D | SER244 |
D | SER247 |
D | ALA248 |
D | PHE298 |
D | HEM501 |
D | HOH640 |
site_id | CC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL D 507 |
Chain | Residue |
D | ARG92 |
D | TYR177 |
D | GLN203 |
Functional Information from PROSITE/UniProt
site_id | PS00086 |
Number of Residues | 10 |
Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGsGVHMCVG |
Chain | Residue | Details |
A | PHE351-GLY360 |