PDB ID: pdb_00007yxt
- Crystal structure of human Indoleamine-2,3-dioxygenase 1 (hIDO1) with different conformations for G261-G265 fragment
- Experimental method: X-RAY DIFFRACTION
- Resolution: 2.48 Å
- Deposition date: 2022-02-16
Number of assemblies: 4
| Structural data | modeled |
|---|---|
| Oligomeric count | 1 |
| label_asym_ids of protein | |
| label_asym_ids of heme | |
| label_asym_ids of the others |
F (GOL |
Each chain information
| auth_asym_id | A |
|---|---|
| Residue indices (Uniprot) | 11-403 (15-403) |
| Mutations (UniProt numbering) | |
| Missing residues | 363LYS-376ALA |
| Structural gaps | Exists |
| Uniprot ID | P14902 →UniprotKB |
| label_asym_ids of heme | E |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.28 Å |
Each chain information
| auth_asym_id | B |
|---|---|
| Residue indices (Uniprot) | 12-402 (15-403) |
| Mutations (UniProt numbering) | |
| Missing residues | 363LYS-376ALA |
| Structural gaps | Exists |
| Uniprot ID | P14902 →UniprotKB |
| label_asym_ids of heme | G |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.10 Å |
| Structural data | modeled |
|---|---|
| Oligomeric count | 1 |
| label_asym_ids of protein | |
| label_asym_ids of heme | |
| label_asym_ids of the others |
M (GOL |
Each chain information
| auth_asym_id | C |
|---|---|
| Residue indices (Uniprot) | 12-402 (15-403) |
| Mutations (UniProt numbering) | |
| Missing residues | 362PRO-376ALA |
| Structural gaps | Exists |
| Uniprot ID | P14902 →UniprotKB |
| label_asym_ids of heme | L |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.18 Å |
Each chain information
| auth_asym_id | D |
|---|---|
| Residue indices (Uniprot) | 10-403 (15-403) |
| Mutations (UniProt numbering) | |
| Missing residues | 363LYS-379THR |
| Structural gaps | Exists |
| Uniprot ID | P14902 →UniprotKB |
| label_asym_ids of heme | N |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.24 Å |

