PDB ID: pdb_00005fw4
- Structure of Thermobifida fusca DyP-type Peroxidase and Activity towards Kraft Lignin and Lignin Model Compounds
- Experimental method: X-RAY DIFFRACTION
- Resolution: 1.8 Å
- Deposition date: 2016-02-11
Number of assemblies: 2
| Structural data | modeled |
|---|---|
| Oligomeric count | 2 |
| label_asym_ids of protein | |
| label_asym_ids of heme | |
| label_asym_ids of the others |
D (OXY  OXY
), D-1 (OXYOXY
)
|
Each chain information
| auth_asym_id | A |
|---|---|
| Residue indices (Uniprot) | 10-391 (1-430) |
| Mutations (UniProt numbering) | |
| Missing residues | 279ASP-292PRO |
| Structural gaps | Exists |
| Uniprot ID | Q47KB1 ￫UniprotKB |
| label_asym_ids of heme | C |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.12 Å |
| auth_asym_id | A |
|---|---|
| Residue indices (Uniprot) | 10-391 (1-430) |
| Mutations (UniProt numbering) | |
| Missing residues | 279ASP-292PRO |
| Structural gaps | Exists |
| Uniprot ID | Q47KB1 ￫UniprotKB |
| label_asym_ids of heme | C-1 |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.11 Å |
| Structural data | modeled |
|---|---|
| Oligomeric count | 2 |
| label_asym_ids of protein | |
| label_asym_ids of heme | |
| label_asym_ids of the others |
F (OXYOXY
), F-1 (OXYOXY
)
|
Each chain information
| auth_asym_id | B |
|---|---|
| Residue indices (Uniprot) | 10-391 (1-430) |
| Mutations (UniProt numbering) | |
| Missing residues | 279ASP-292PRO |
| Structural gaps | Exists |
| Uniprot ID | Q47KB1 ￫UniprotKB |
| label_asym_ids of heme | E |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.13 Å |
| auth_asym_id | B |
|---|---|
| Residue indices (Uniprot) | 10-391 (1-430) |
| Mutations (UniProt numbering) | |
| Missing residues | 279ASP-292PRO |
| Structural gaps | Exists |
| Uniprot ID | Q47KB1 ￫UniprotKB |
| label_asym_ids of heme | E-1 |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.11 Å |