PDB ID: pdb_00006e45
- CRYSTAL STRUCTURE OF HUMAN INDOLEAMINE 2,3-DIOXYGENASE 1 (IDO1) free enzyme in the ferrous state
- Experimental method: X-RAY DIFFRACTION
- Resolution: 2 Å
- Deposition date: 2018-07-16
Number of assemblies: 4
| Structural data | including_not_modeled |
|---|---|
| Oligomeric count | 1 |
| label_asym_ids of protein | |
| label_asym_ids of heme | |
| label_asym_ids of the others |
F (GOL  GOL
), G (GOLGOL
)
|
| Structural data | modeled |
|---|---|
| Oligomeric count | 1 |
| label_asym_ids of protein | |
| label_asym_ids of heme | |
| label_asym_ids of the others |
I (PO4 PO4
)
|
Each chain information
| auth_asym_id | B |
|---|---|
| Residue indices (Uniprot) | 14-401 (15-403) |
| Mutations (UniProt numbering) | |
| Missing residues | 361GLN-375GLU |
| Structural gaps | Exists |
| Uniprot ID | P14902 ￫UniprotKB |
| label_asym_ids of heme | H |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.20 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 | C |
|---|---|
| Residue indices (Uniprot) | 14-402 (15-403) |
| Mutations (UniProt numbering) | |
| Missing residues | 361GLN-379THR |
| Structural gaps | Exists |
| Uniprot ID | P14902 ￫UniprotKB |
| label_asym_ids of heme | J |
| 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 |
L (PO4PO4
), M (PO4PO4
), N (GOLGOL
), O (GOLGOL
), P (GOLGOL
)
|
Each chain information
| auth_asym_id | D |
|---|---|
| Residue indices (Uniprot) | 14-401 (15-403) |
| Mutations (UniProt numbering) | |
| Missing residues | 361GLN-379THR |
| Structural gaps | Exists |
| Uniprot ID | P14902 ￫UniprotKB |
| label_asym_ids of heme | K |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.09 Å |