PDB ID: pdb_00003bk9
- H55A mutant of tryptophan 2,3-dioxygenase from Xanthomonas campestris
- Experimental method: X-RAY DIFFRACTION
- Resolution: 2.15 Å
- Deposition date: 2007-12-06
Number of assemblies: 2
Each chain information
| auth_asym_id | A |
|---|---|
| Residue indices (Uniprot) | 7-283 (1-298) |
| Mutations (UniProt numbering) | |
| Uniprot ID | Q8PDA8 →UniprotKB |
| label_asym_ids of heme | J |
| Available structure | PDB |
| auth_asym_id | B |
|---|---|
| Residue indices (Uniprot) | 7-286 (1-298) |
| Mutations (UniProt numbering) | |
| Uniprot ID | Q8PDA8 →UniprotKB |
| label_asym_ids of heme | M |
| Available structure | PDB |
| auth_asym_id | C |
|---|---|
| Residue indices (Uniprot) | 7-282 (1-298) |
| Mutations (UniProt numbering) | |
| Missing residues | 187TYR-190ARG |
| Structural gaps | Exists |
| Uniprot ID | Q8PDA8 →UniprotKB |
| label_asym_ids of heme | Q |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.15 Å |
Each chain information
| auth_asym_id | E |
|---|---|
| Residue indices (Uniprot) | 23-282 (1-298) |
| Mutations (UniProt numbering) | |
| Uniprot ID | Q8PDA8 →UniprotKB |
| label_asym_ids of heme | V |
| Available structure | PDB |
| auth_asym_id | F |
|---|---|
| Residue indices (Uniprot) | 23-283 (1-298) |
| Mutations (UniProt numbering) | |
| Missing residues | 188GLN-198ALA |
| Structural gaps | Exists |
| Uniprot ID | Q8PDA8 →UniprotKB |
| label_asym_ids of heme | Y |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 1.21 Å |
| auth_asym_id | G |
|---|---|
| Residue indices (Uniprot) | 21-282 (1-298) |
| Mutations (UniProt numbering) | |
| Uniprot ID | Q8PDA8 →UniprotKB |
| label_asym_ids of heme | AA |
| Available structure | PDB |
| auth_asym_id | H |
|---|---|
| Residue indices (Uniprot) | 22-283 (1-298) |
| Mutations (UniProt numbering) | |
| Missing residues | 187TYR-191ASP |
| Structural gaps | Exists |
| Uniprot ID | Q8PDA8 →UniprotKB |
| label_asym_ids of heme | CA |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.22 Å |

