5Y5L
Time-resolved SFX structure of cytochrome P450nor: dark-2 data in the absence of NADH (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 | 23 |
Details | binding site for residue HEM A 501 |
Chain | Residue |
A | PHE86 |
A | MET244 |
A | MET247 |
A | GLY344 |
A | PHE345 |
A | GLY346 |
A | PHE347 |
A | HIS350 |
A | CYS352 |
A | ILE353 |
A | ALA354 |
A | VAL87 |
A | HOH608 |
A | HOH656 |
A | HOH683 |
A | HOH716 |
A | HIS94 |
A | ARG98 |
A | ILE153 |
A | LEU236 |
A | ALA239 |
A | GLY240 |
A | THR243 |
site_id | AC2 |
Number of Residues | 20 |
Details | binding site for residue HEM B 501 |
Chain | Residue |
B | PHE86 |
B | VAL87 |
B | HIS94 |
B | ARG98 |
B | LEU236 |
B | GLY240 |
B | THR243 |
B | MET244 |
B | GLY344 |
B | PHE345 |
B | GLY346 |
B | PHE347 |
B | HIS350 |
B | CYS352 |
B | ILE353 |
B | ALA354 |
B | HOH601 |
B | HOH608 |
B | HOH610 |
B | HOH693 |
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) |