PDB ID: pdb_00001h7k
- Formation of a tyrosyl radical intermediate in Proteus mirabilis catalase by directed mutagenesis and consequences for nucleotide reactivity
- Experimental method: X-RAY DIFFRACTION
- Resolution: 2.4 Å
- Deposition date: 2001-07-08
Number of assemblies: 1
| Structural data | modeled |
|---|---|
| Oligomeric count | 4 |
| label_asym_ids of protein | |
| label_asym_ids of heme | |
| label_asym_ids of the others |
C (ACT  ACT
), C-1 (ACTACT
), C-2 (ACTACT
), C-3 (ACTACT
), D (SO4 SO4
), D-1 (SO4SO4
), D-2 (SO4SO4
), D-3 (SO4SO4
)
|
Each chain information
| auth_asym_id | A |
|---|---|
| Residue indices (Uniprot) | 4-478 (2-484) |
| Mutations (UniProt numbering) | |
| Missing residues | 53MET-53MET |
| Structural gaps | Exists |
| Nonstandard amino acids |
 OMT
|
| Uniprot ID | P42321 ￫UniprotKB |
| label_asym_ids of heme | B |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.09 Å |
| auth_asym_id | A |
|---|---|
| Residue indices (Uniprot) | 4-478 (2-484) |
| Mutations (UniProt numbering) | |
| Missing residues | 53MET-53MET |
| Structural gaps | Exists |
| Nonstandard amino acids |
OMT
|
| Uniprot ID | P42321 ￫UniprotKB |
| label_asym_ids of heme | B-1 |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.09 Å |
| auth_asym_id | A |
|---|---|
| Residue indices (Uniprot) | 4-478 (2-484) |
| Mutations (UniProt numbering) | |
| Missing residues | 53MET-53MET |
| Structural gaps | Exists |
| Nonstandard amino acids |
OMT
|
| Uniprot ID | P42321 ￫UniprotKB |
| label_asym_ids of heme | B-2 |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.09 Å |
| auth_asym_id | A |
|---|---|
| Residue indices (Uniprot) | 4-478 (2-484) |
| Mutations (UniProt numbering) | |
| Missing residues | 53MET-53MET |
| Structural gaps | Exists |
| Nonstandard amino acids |
OMT
|
| Uniprot ID | P42321 ￫UniprotKB |
| label_asym_ids of heme | B-3 |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.09 Å |