PDB ID: pdb_00001smi
- A single mutation of P450 BM3 induces the conformational rearrangement seen upon substrate-binding in wild-type enzyme
- Experimental method: X-RAY DIFFRACTION
- Resolution: 2 Å
- Deposition date: 2004-03-09
Number of assemblies: 2
| Structural data | modeled |
|---|---|
| Oligomeric count | 1 |
| label_asym_ids of protein | |
| label_asym_ids of heme | |
| label_asym_ids of the others |
Each chain information
| auth_asym_id | A |
|---|---|
| Residue indices (Uniprot) | 1-456 (2-472) |
| Mutations (UniProt numbering) | |
| Missing residues | 108SER-108SER:193PRO-203ARG:226SER-230SER |
| Structural gaps | Exists |
| Uniprot ID | P14779 ￫UniprotKB |
| label_asym_ids of heme | C |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.16 Å |
| Structural data | modeled |
|---|---|
| Oligomeric count | 1 |
| label_asym_ids of protein | |
| label_asym_ids of heme | |
| label_asym_ids of the others |
Each chain information
| auth_asym_id | B |
|---|---|
| Residue indices (Uniprot) | 2-458 (2-472) |
| Mutations (UniProt numbering) | |
| Missing residues | 227GLY-228GLU |
| Structural gaps | Exists |
| Uniprot ID | P14779 ￫UniprotKB |
| label_asym_ids of heme | D |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.15 Å |