4TRI
X-ray crystal structure of CYP142A2 from Mycobacterium smegmatis, complexed with cholesterol sulfate.
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 |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0006707 | biological_process | cholesterol catabolic process |
| B | 0008202 | biological_process | steroid metabolic process |
| B | 0008203 | biological_process | cholesterol metabolic process |
| B | 0008395 | molecular_function | steroid hydroxylase activity |
| 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 | 0036199 | molecular_function | cholest-4-en-3-one 26-monooxygenase activity |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 23 |
| Details | binding site for residue HEM A 501 |
| Chain | Residue |
| A | GLU56 |
| A | THR238 |
| A | VAL280 |
| A | ARG285 |
| A | ALA335 |
| A | PHE336 |
| A | GLY337 |
| A | PHE338 |
| A | HIS341 |
| A | CYS343 |
| A | LEU344 |
| A | ILE79 |
| A | GLY345 |
| A | LEU348 |
| A | C3S502 |
| A | HOH667 |
| A | HIS86 |
| A | ARG90 |
| A | PHE97 |
| A | ILE141 |
| A | GLY233 |
| A | GLY234 |
| A | THR237 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue C3S A 502 |
| Chain | Residue |
| A | TYR77 |
| A | MET179 |
| A | LEU229 |
| A | HEM501 |
| A | HOH812 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 503 |
| Chain | Residue |
| A | GLU122 |
| A | LEU145 |
| A | GLY146 |
| A | ARG196 |
| A | ASP203 |
| A | HIS402 |
| A | HOH601 |
| A | HOH614 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue C3S B 501 |
| Chain | Residue |
| B | TYR77 |
| B | MET179 |
| B | LEU229 |
| B | PHE382 |
| B | HEM502 |
| B | HOH746 |
| B | HOH924 |
| site_id | AC5 |
| Number of Residues | 23 |
| Details | binding site for residue HEM B 502 |
| Chain | Residue |
| B | GLU56 |
| B | ILE79 |
| B | HIS86 |
| B | ARG90 |
| B | PHE97 |
| B | ILE230 |
| B | GLY233 |
| B | THR237 |
| B | THR238 |
| B | THR241 |
| B | PRO279 |
| B | VAL280 |
| B | ARG285 |
| B | ALA335 |
| B | PHE336 |
| B | GLY337 |
| B | PHE338 |
| B | HIS341 |
| B | CYS343 |
| B | LEU344 |
| B | GLY345 |
| B | C3S501 |
| B | HOH669 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 503 |
| Chain | Residue |
| B | LEU145 |
| B | GLY146 |
| B | GLU151 |
| B | VAL192 |
| B | ARG196 |
| B | ASP203 |
Functional Information from PROSITE/UniProt
| site_id | PS00086 |
| Number of Residues | 10 |
| Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGfGTHFCLG |
| Chain | Residue | Details |
| A | PHE336-GLY345 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"23489718","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25210044","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2YOO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ZBY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4TRI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4UAX","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
