Research workbench
Structure of human neuronal nitric oxide synthase R354A/G357D mutant heme domain in complex with 6-(4-(DIMETHYLAMINO)BUT-1-yn-1-yl)-4- methylpyridin-2-amine
Analyse Structure of human neuronal nitric oxide synthase R354A/G357D mutant heme… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7US7
- Type
- protein
- Length
- 1,663 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nitric oxide synthase, brain
- EC
- 1.14.13.39
- UniProt
- P29475
- Ligands
- HEM, H4B, O5X, ZN
- Pockets
- 20 · best druggability 0.88
Structure
x-ray diffraction · 3 distinct chains · 40% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | Nitric oxide synthase, brain (EC 1.14.13.39) | protein | 418 | 40% helix, 15% strand | P29475 |
| B | Nitric oxide synthase, brain (EC 1.14.13.39) | protein | 414 | 40% helix, 15% strand | P29475 |
| C | Nitric oxide synthase, brain (EC 1.14.13.39) | protein | 413 | 40% helix, 15% strand | P29475 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 4 copies · chains A, B, C, D
- H4B · 5,6,7,8-tetrahydrobiopterin · ligand · 4 copies · chains A, B, C, D
- O5X · 6-[4-(dimethylamino)but-1-yn-1-yl]-4-methylpyridin-2-amine · ligand · 4 copies · chains A, B, C, D
- ZN · Zinc ion · metal · 2 copies · chains A, B, C, D
- GOL · Glycerol · additive · 7 copies · chains A, D, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 779 | 0.88 | 0.91 | 103 | HEM, H4B, O5X |
| 2 | 1041 | 0.85 | 0.86 | 87 | HEM, H4B, O5X |
| 3 | 969 | 0.85 | 0.86 | 93 | HEM, H4B, O5X |
| 4 | 345 | 0.80 | 0.90 | 49 | HEM, H4B, O5X |
| 5 | 256 | 0.64 | 0.82 | 34 | GOL |
Interfaces
4 interfaces between chains.
- A–B · 2756 Ų buried · 39 hydrogen bonds · protein-protein
- C–D · 2733 Ų buried · 41 hydrogen bonds · protein-protein
- A–D · 886 Ų buried · 10 hydrogen bonds · protein-protein
- B–D · 123 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 7US7 · Structure of human neuronal nitric oxide synthase R354A/G357D mutant heme domain in… · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P29475
- Elsewhere: RCSB PDB 7US7 · PDBe 7US7 · UniProt P29475
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