4EGO
The X-ray crystal structure of CYP199A4 in complex with indole-6-carboxylic acid
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004497 | molecular_function | monooxygenase activity |
A | 0005506 | molecular_function | iron ion binding |
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 | 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 | 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 |
D | 0004497 | molecular_function | monooxygenase activity |
D | 0005506 | molecular_function | iron ion binding |
D | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
D | 0020037 | molecular_function | heme binding |
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 | 1F1502 |
A | LEU98 |
A | HOH606 |
A | HOH610 |
A | HIS105 |
A | ARG109 |
A | PHE160 |
A | ALA248 |
A | GLY249 |
A | THR252 |
A | THR253 |
site_id | AC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE 1F1 A 502 |
Chain | Residue |
A | ARG92 |
A | SER95 |
A | LEU98 |
A | PHE182 |
A | SER244 |
A | SER247 |
A | ALA248 |
A | PHE298 |
A | HEM501 |
A | HOH637 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE 1F1 A 503 |
Chain | Residue |
A | GLU153 |
A | GLY179 |
A | ASP251 |
A | ARG391 |
A | HOH875 |
A | HOH895 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE 1F1 A 504 |
Chain | Residue |
A | PRO90 |
A | ARG92 |
A | PRO94 |
C | ARG142 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 505 |
Chain | Residue |
A | ARG109 |
A | SER113 |
A | GOL507 |
A | HOH789 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 506 |
Chain | Residue |
A | ARG78 |
A | LYS86 |
A | HOH911 |
A | HOH912 |
D | THR40 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 507 |
Chain | Residue |
A | SER113 |
A | LEU116 |
A | SER117 |
A | VAL359 |
A | GLN361 |
A | SO4505 |
A | HOH802 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 508 |
Chain | Residue |
A | SER334 |
A | ASP335 |
A | ASP340 |
A | ARG343 |
A | HOH786 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL A 509 |
Chain | Residue |
A | ARG92 |
A | TYR177 |
A | GLN203 |
A | HOH926 |
site_id | BC1 |
Number of Residues | 22 |
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 | ALA364 |
B | 1F1502 |
B | HOH606 |
B | HOH624 |
site_id | BC2 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE 1F1 B 502 |
Chain | Residue |
B | ARG92 |
B | SER95 |
B | LEU98 |
B | PHE182 |
B | PHE185 |
B | SER244 |
B | SER247 |
B | ALA248 |
B | PHE298 |
B | HEM501 |
B | HOH639 |
site_id | BC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE 1F1 B 503 |
Chain | Residue |
B | GLU153 |
B | LEU175 |
B | GLY179 |
B | ASP251 |
B | ARG391 |
B | ASN393 |
B | HOH656 |
site_id | BC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 B 504 |
Chain | Residue |
B | ARG109 |
B | SER113 |
B | GOL505 |
B | HOH628 |
B | HOH691 |
B | HOH838 |
B | HOH869 |
C | LYS114 |
site_id | BC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL B 505 |
Chain | Residue |
B | SER113 |
B | LEU116 |
B | SER117 |
B | VAL359 |
B | GLN361 |
B | LEU362 |
B | SO4504 |
B | HOH882 |
site_id | BC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL B 506 |
Chain | Residue |
A | ARG60 |
A | HOH856 |
B | ARG60 |
site_id | BC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL B 507 |
Chain | Residue |
B | SER334 |
B | ASP335 |
B | ASP340 |
B | ARG343 |
B | HOH876 |
site_id | BC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL B 508 |
Chain | Residue |
B | ARG92 |
B | TYR177 |
B | GLN203 |
site_id | BC9 |
Number of Residues | 21 |
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 | PHE298 |
C | ARG300 |
C | GLY350 |
C | PHE351 |
C | GLY352 |
C | HIS356 |
C | CYS358 |
C | VAL359 |
C | GLY360 |
C | ALA364 |
C | 1F1502 |
C | HOH610 |
C | HOH620 |
site_id | CC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE 1F1 C 502 |
Chain | Residue |
C | ARG92 |
C | SER95 |
C | PHE182 |
C | SER244 |
C | SER247 |
C | ALA248 |
C | PHE298 |
C | HEM501 |
C | HOH624 |
site_id | CC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE 1F1 C 503 |
Chain | Residue |
C | LEU175 |
C | PRO176 |
C | ASP251 |
C | ARG391 |
C | HOH734 |
C | HOH814 |
site_id | CC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 C 504 |
Chain | Residue |
B | LYS114 |
C | ARG109 |
C | SER113 |
C | GOL507 |
C | HOH647 |
site_id | CC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 C 505 |
Chain | Residue |
B | ARG107 |
B | HOH649 |
B | HOH726 |
C | ARG107 |
C | HOH638 |
site_id | CC5 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE SO4 C 506 |
Chain | Residue |
C | ARG60 |
site_id | CC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL C 507 |
Chain | Residue |
C | SER113 |
C | LEU116 |
C | SER117 |
C | VAL359 |
C | GLN361 |
C | LEU362 |
C | SO4504 |
site_id | CC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL C 508 |
Chain | Residue |
C | ARG92 |
C | TYR177 |
C | GLN203 |
site_id | CC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE 1F1 D 501 |
Chain | Residue |
C | TYR262 |
C | ILE384 |
C | HOH800 |
D | ARG266 |
D | ILE384 |
D | HOH713 |
site_id | CC9 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE HEM D 502 |
Chain | Residue |
D | ILE97 |
D | LEU98 |
D | HIS105 |
D | ARG109 |
D | PHE160 |
D | LEU245 |
D | ALA248 |
D | GLY249 |
D | THR252 |
D | THR253 |
D | PHE298 |
D | ARG300 |
D | GLY350 |
D | PHE351 |
D | GLY352 |
D | VAL355 |
D | HIS356 |
D | CYS358 |
D | VAL359 |
D | GLY360 |
D | ALA364 |
D | 1F1503 |
D | HOH604 |
D | HOH625 |
site_id | DC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE 1F1 D 503 |
Chain | Residue |
D | ARG92 |
D | SER95 |
D | PHE182 |
D | PHE185 |
D | SER244 |
D | SER247 |
D | ALA248 |
D | PHE298 |
D | HEM502 |
D | HOH620 |
site_id | DC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 D 504 |
Chain | Residue |
A | LYS114 |
A | HOH766 |
D | ARG109 |
D | SER113 |
D | GOL506 |
D | HOH813 |
site_id | DC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 D 505 |
Chain | Residue |
A | ARG107 |
A | HOH751 |
D | ARG107 |
D | HOH650 |
D | HOH709 |
D | HOH802 |
site_id | DC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL D 506 |
Chain | Residue |
D | SER113 |
D | LEU116 |
D | SER117 |
D | VAL359 |
D | GLN361 |
D | SO4504 |
site_id | DC5 |
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 |