PDB ID: pdb_00003dwj
- Heme-proximal W188H mutant of inducible nitric oxide synthase
- Experimental method: X-RAY DIFFRACTION
- Resolution: 2.75 Å
- Deposition date: 2008-07-22
Number of assemblies: 2
| Structural data | modeled |
|---|---|
| Oligomeric count | 2 |
| label_asym_ids of protein | |
| label_asym_ids of heme | |
| label_asym_ids of the others |
C (SO4  SO4
), C-1 (SO4SO4
), D (NH4 NH4
), D-1 (NH4NH4
), F (H4B H4B
), F-1 (H4BH4B
)
|
Each chain information
| auth_asym_id | A |
|---|---|
| Residue indices (Uniprot) | 77-495 (66-496) |
| Mutations (UniProt numbering) | |
| Missing residues | 101ASP-111GLY |
| Structural gaps | Exists |
| Uniprot ID | P29477 ￫UniprotKB |
| label_asym_ids of heme | E |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.13 Å |
| auth_asym_id | A |
|---|---|
| Residue indices (Uniprot) | 77-495 (66-496) |
| Mutations (UniProt numbering) | |
| Missing residues | 101ASP-111GLY |
| Structural gaps | Exists |
| Uniprot ID | P29477 ￫UniprotKB |
| label_asym_ids of heme | E-1 |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.13 Å |
| Structural data | modeled |
|---|---|
| Oligomeric count | 2 |
| label_asym_ids of protein | |
| label_asym_ids of heme | |
| label_asym_ids of the others |
G (NH4NH4
), G-1 (NH4NH4
), I (H4BH4B
), I-1 (H4BH4B
)
|
Each chain information
| auth_asym_id | B |
|---|---|
| Residue indices (Uniprot) | 77-496 (66-496) |
| Mutations (UniProt numbering) | |
| Missing residues | 101ASP-108SER |
| Structural gaps | Exists |
| Uniprot ID | P29477 ￫UniprotKB |
| label_asym_ids of heme | H |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.14 Å |
| auth_asym_id | B |
|---|---|
| Residue indices (Uniprot) | 77-496 (66-496) |
| Mutations (UniProt numbering) | |
| Missing residues | 101ASP-108SER |
| Structural gaps | Exists |
| Uniprot ID | P29477 ￫UniprotKB |
| label_asym_ids of heme | H-1 |
| Available structure | PDB and Modeled |
| RMSD of experimental residues after energy minimization | 0.14 Å |