5Y5M
SFX structure of cytochrome P450nor: a complete dark data without pump laser (resting state)
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 | 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 |
| A | 0102199 | molecular_function | nitric oxide reductase (NAD(P)H) activity |
| 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 | 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 |
| B | 0102199 | molecular_function | nitric oxide reductase (NAD(P)H) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | binding site for residue HEM A 501 |
| Chain | Residue |
| A | PHE86 |
| A | MET247 |
| A | GLY344 |
| A | PHE345 |
| A | GLY346 |
| A | PHE347 |
| A | HIS350 |
| A | CYS352 |
| A | ILE353 |
| A | ALA354 |
| A | HOH604 |
| A | VAL87 |
| A | HOH644 |
| A | HOH673 |
| A | HOH692 |
| A | HIS94 |
| A | ARG98 |
| A | ILE153 |
| A | LEU236 |
| A | GLY240 |
| A | THR243 |
| A | MET244 |
| site_id | AC2 |
| Number of Residues | 21 |
| Details | binding site for residue HEM B 501 |
| Chain | Residue |
| B | PHE86 |
| B | VAL87 |
| B | HIS94 |
| B | ARG98 |
| B | ILE153 |
| B | LEU236 |
| B | GLY240 |
| B | MET244 |
| B | MET247 |
| B | GLY344 |
| B | PHE345 |
| B | GLY346 |
| B | PHE347 |
| B | HIS350 |
| B | CYS352 |
| B | ILE353 |
| B | ALA354 |
| B | HOH603 |
| B | HOH615 |
| B | HOH619 |
| B | HOH729 |
Functional Information from PROSITE/UniProt
| site_id | PS00086 |
| Number of Residues | 10 |
| Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGfGDHRCIA |
| Chain | Residue | Details |
| A | PHE345-ALA354 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | BINDING: axial binding residue |
| Chain | Residue | Details |
| A | CYS352 | |
| B | CYS352 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: N-acetylalanine => ECO:0000269|PubMed:9010754 |
| Chain | Residue | Details |
| A | ALA2 | |
| B | ALA2 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 473 |
| Chain | Residue | Details |
| A | THR243 | steric role |
| A | SER286 | proton shuttle (general acid/base) |
| A | CYS352 | activator, metal ligand |
| A | ASP393 | proton shuttle (general acid/base) |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 473 |
| Chain | Residue | Details |
| B | THR243 | steric role |
| B | SER286 | proton shuttle (general acid/base) |
| B | CYS352 | activator, metal ligand |
| B | ASP393 | proton shuttle (general acid/base) |
