PDB ID: pdb_00005tft
- Structure of cytochrome P450 2D6 (CYP2D6) BACE1 inhibitor complex
- Experimental method: X-RAY DIFFRACTION
- Resolution: 2.71 Å
- Deposition date: 2016-09-26
Number of assemblies: 4
| Structural data | PDB |
|---|---|
| Oligomeric count | 1 |
| label_asym_ids of protein | |
| label_asym_ids of heme | |
| label_asym_ids of the others |
F (ZN  ZN
), G (ZNZN
), H (P6U P6U
)
|
| Structural data | modeled |
|---|---|
| Oligomeric count | 1 |
| label_asym_ids of protein | |
| label_asym_ids of heme | |
| label_asym_ids of the others |
J (ZNZN
), K (P6UP6U
)
|
Each chain information
| auth_asym_id | B |
|---|---|
| Residue indices (Uniprot) | 31-497 (34-497) |
| Mutations (UniProt numbering) | |
| Missing residues | 40LEU-43LEU:144LEU-146LYS |
| Structural gaps | Exists |
| Uniprot ID | P10635 ￫UniprotKB |
| label_asym_ids of heme | I |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.12 Å |
| Structural data | modeled |
|---|---|
| Oligomeric count | 1 |
| label_asym_ids of protein | |
| label_asym_ids of heme | |
| label_asym_ids of the others |
M (ZNZN
), N (P6UP6U
)
|
Each chain information
| auth_asym_id | C |
|---|---|
| Residue indices (Uniprot) | 33-497 (34-497) |
| Mutations (UniProt numbering) | |
| Missing residues | 40LEU-51PHE:144LEU-149LEU |
| Structural gaps | Exists |
| Uniprot ID | P10635 ￫UniprotKB |
| label_asym_ids of heme | L |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.13 Å |
| Structural data | modeled |
|---|---|
| Oligomeric count | 1 |
| label_asym_ids of protein | |
| label_asym_ids of heme | |
| label_asym_ids of the others |
P (ZNZN
), Q (P6UP6U
)
|
Each chain information
| auth_asym_id | D |
|---|---|
| Residue indices (Uniprot) | 33-497 (34-497) |
| Mutations (UniProt numbering) | |
| Missing residues | 40LEU-51PHE |
| Structural gaps | Exists |
| Uniprot ID | P10635 ￫UniprotKB |
| label_asym_ids of heme | O |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.11 Å |