4APY
Ethylene glycol-bound form of P450 CYP125A3 from Mycobacterium smegmatis
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 | 0006707 | biological_process | cholesterol catabolic process |
| A | 0008202 | biological_process | steroid metabolic process |
| A | 0008203 | biological_process | cholesterol metabolic process |
| A | 0008395 | molecular_function | steroid hydroxylase activity |
| 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 | 0036199 | molecular_function | cholest-4-en-3-one 26-monooxygenase activity |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 1416 |
| Chain | Residue |
| A | GLU20 |
| A | LYS63 |
| A | PRO348 |
| A | HIS349 |
| A | THR355 |
| A | HOH2095 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 1417 |
| Chain | Residue |
| A | GLU283 |
| A | ASN371 |
| A | ASN375 |
| A | TYR277 |
| A | ARG281 |
| A | PRO282 |
| site_id | AC3 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE HEM A 1418 |
| Chain | Residue |
| A | LEU99 |
| A | LEU100 |
| A | HIS107 |
| A | ARG111 |
| A | ALA251 |
| A | GLY252 |
| A | THR255 |
| A | THR256 |
| A | PRO295 |
| A | PHE299 |
| A | ARG301 |
| A | TYR324 |
| A | GLY351 |
| A | PHE352 |
| A | GLY353 |
| A | GLY354 |
| A | ALA357 |
| A | HIS358 |
| A | CYS360 |
| A | ILE361 |
| A | GLY362 |
| A | EDO1423 |
| A | HOH2105 |
| A | HOH2277 |
| A | HOH2314 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 1419 |
| Chain | Residue |
| A | HIS262 |
| A | ARG392 |
| A | HOH2245 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 1420 |
| Chain | Residue |
| A | VAL24 |
| A | TRP292 |
| A | HIS338 |
| A | HOH2272 |
| A | HOH2296 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 1421 |
| Chain | Residue |
| A | ILE80 |
| A | PHE299 |
| A | EDO1423 |
| A | HOH2135 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 1422 |
| Chain | Residue |
| A | SER75 |
| A | PRO76 |
| A | ASP93 |
| A | ARG96 |
| A | HOH2134 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 1423 |
| Chain | Residue |
| A | MET247 |
| A | ALA251 |
| A | HEM1418 |
| A | EDO1421 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 1424 |
| Chain | Residue |
| A | CYS155 |
| A | GLU156 |
| A | ASN181 |
| A | HOH2211 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 1425 |
| Chain | Residue |
| A | ASP195 |
| A | ASP195 |
| A | PRO196 |
| A | PRO196 |
| A | ALA197 |
| A | ALA197 |
| A | MET198 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 1427 |
| Chain | Residue |
| A | PHE10 |
| A | ASP11 |
| A | ASP14 |
| A | HOH2030 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"23489718","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4APY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5DQN","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
