PDB ID: pdb_00007a62
- Structure of human indoleamine-2,3-dioxygenase 1 (hIDO1) with a complete JK loop
- Experimental method: X-RAY DIFFRACTION
- Resolution: 2.43796448682 Å
- Deposition date: 2020-08-24
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 |
E (GOL  GOL
)
|
Each chain information
| auth_asym_id | A |
|---|---|
| Residue indices (Uniprot) | 12-401 (15-403) |
| Mutations (UniProt numbering) | |
| Missing residues | 363LYS-378GLY |
| Structural gaps | Exists |
| Uniprot ID | P14902 ￫UniprotKB |
| label_asym_ids of heme | F |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.24 Å |
| Structural data | modeled |
|---|---|
| Oligomeric count | 1 |
| label_asym_ids of protein | |
| label_asym_ids of heme | |
| label_asym_ids of the others |
G (GOLGOL
), H (GOLGOL
)
|
Each chain information
| auth_asym_id | B |
|---|---|
| Residue indices (Uniprot) | 11-403 (15-403) |
| Mutations (UniProt numbering) | |
| Missing residues | 363LYS-377LYS |
| Structural gaps | Exists |
| Uniprot ID | P14902 ￫UniprotKB |
| label_asym_ids of heme | I |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.13 Å |
| Structural data | PDB |
|---|---|
| Oligomeric count | 1 |
| label_asym_ids of protein | |
| label_asym_ids of heme | |
| label_asym_ids of the others |
J (CL CL
), K (GOLGOL
), L (GOLGOL
)
|
| Structural data | modeled |
|---|---|
| Oligomeric count | 1 |
| label_asym_ids of protein | |
| label_asym_ids of heme | |
| label_asym_ids of the others |
N (GOLGOL
), O (CLCL
), P (GOLGOL
)
|
Each chain information
| auth_asym_id | D |
|---|---|
| Residue indices (Uniprot) | 11-401 (15-403) |
| Mutations (UniProt numbering) | |
| Missing residues | 363LYS-378GLY |
| Structural gaps | Exists |
| Uniprot ID | P14902 ￫UniprotKB |
| label_asym_ids of heme | Q |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 1.18 Å |