8TDP
Time-resolved SFX-XFEL crystal structure of CYP121 bound with cYY reacted with peracetic acid for 200 milliseconds
Replaces: 7RUKFunctional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006707 | biological_process | cholesterol catabolic process |
| A | 0008395 | molecular_function | steroid hydroxylase activity |
| A | 0009975 | molecular_function | cyclase 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 | 0016717 | molecular_function | oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water |
| 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 | 0070025 | molecular_function | carbon monoxide binding |
Functional Information from PROSITE/UniProt
| site_id | PS00086 |
| Number of Residues | 10 |
| Details | CYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGrGQHFCPG |
| Chain | Residue | Details |
| A | PHE338-GLY347 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17028183, ECO:0000269|PubMed:19416919 |
| Chain | Residue | Details |
| A | THR77 | |
| A | SER237 | |
| A | LYS301 | |
| A | GLN385 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ASN85 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12435731, ECO:0000269|PubMed:17028183, ECO:0000269|PubMed:18818197, ECO:0000269|PubMed:19416919, ECO:0000269|PubMed:22890978, ECO:0000269|PubMed:23620594 |
| Chain | Residue | Details |
| A | ARG286 | |
| A | HIS343 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | BINDING: axial binding residue |
| Chain | Residue | Details |
| A | CYS345 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | SITE: Participates in a stacking interactions with the tyrosyl of cYY |
| Chain | Residue | Details |
| A | PHE168 | |
| A | TRP182 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | SITE: Important for the position of heme |
| Chain | Residue | Details |
| A | PRO346 |
