6F88
Crystal structure of cytochrome P450 CYP260A1 (S276N) bound with progesterone
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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 27 |
Details | binding site for residue HEM A 501 |
Chain | Residue |
A | LEU73 |
A | THR233 |
A | THR234 |
A | LEU237 |
A | ASN276 |
A | GLY278 |
A | VAL279 |
A | ARG281 |
A | VAL332 |
A | PHE333 |
A | GLY334 |
A | ALA74 |
A | GLY335 |
A | HIS338 |
A | CYS340 |
A | VAL341 |
A | GLY342 |
A | STR502 |
A | HOH785 |
A | HOH850 |
A | HIS81 |
A | ARG85 |
A | TYR88 |
A | PHE92 |
A | LEU226 |
A | GLY229 |
A | GLY230 |
site_id | AC2 |
Number of Residues | 9 |
Details | binding site for residue STR A 502 |
Chain | Residue |
A | LEU69 |
A | SER225 |
A | ASN276 |
A | PHE277 |
A | GLY278 |
A | VAL382 |
A | HEM501 |
A | HOH613 |
A | HOH788 |
site_id | AC3 |
Number of Residues | 28 |
Details | binding site for residue HEM B 501 |
Chain | Residue |
B | LEU73 |
B | ALA74 |
B | HIS81 |
B | ARG85 |
B | SER225 |
B | LEU226 |
B | GLY229 |
B | GLY230 |
B | THR233 |
B | THR234 |
B | LEU237 |
B | SER275 |
B | ASN276 |
B | GLY278 |
B | VAL279 |
B | ARG281 |
B | VAL332 |
B | PHE333 |
B | GLY334 |
B | HIS338 |
B | CYS340 |
B | VAL341 |
B | GLY342 |
B | LEU345 |
B | ALA346 |
B | STR502 |
B | HOH613 |
B | HOH630 |
site_id | AC4 |
Number of Residues | 8 |
Details | binding site for residue STR B 502 |
Chain | Residue |
B | LEU69 |
B | SER225 |
B | ASN276 |
B | GLY278 |
B | VAL382 |
B | HEM501 |
B | HOH656 |
B | HOH657 |
Functional Information from PROSITE/UniProt
site_id | PS00086 |
Number of Residues | 10 |
Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGgGAHFCVG |
Chain | Residue | Details |
A | PHE333-GLY342 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:27878817, ECO:0000269|PubMed:29509407, ECO:0007744|PDB:5LIV, ECO:0007744|PDB:6F85, ECO:0007744|PDB:6F88, ECO:0007744|PDB:6F8A, ECO:0007744|PDB:6F8C |
Chain | Residue | Details |
A | CYS340 | |
B | CYS340 |