Research workbench
P332G, A333S double mutant of the bacillus subtilis nitric oxide synthase
Analyse P332G, A333S double mutant of the bacillus subtilis nitric oxide synthase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2AN2
- Type
- protein
- Length
- 360 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- P332G A333S double mutant of nitric oxide synthase from bacillus subtilis
- EC
- 1.14.13.39
- UniProt
- O34453
- Ligands
- ARG, HEM, H4B
- Pockets
- 3 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | P332G A333S double mutant of nitric oxide synthase from bacillus subtilis (EC 1.14.13.39) | protein | 360 | 43% helix, 14% strand | O34453 |
Ligands and binding sites
- ARG · Arginine · ligand · chains A
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
- H4B · 5,6,7,8-tetrahydrobiopterin · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 669 | 0.78 | 0.83 | 58 | ARG, HEM |
| 2 | 60 | 0.32 | 0.76 | 16 | empty |
| 3 | 72 | 0.31 | 0.74 | 16 | empty |
Compared structures
- 2AN2 · P332G, A333S Double mutant of the Bacillus subtilis Nitric Oxide Synthase · the same entry in another collection · chain A against A, TM-score 1.00
- O34453 · AlphaFold monomer V2.0 prediction for nitric oxide synthase oxygenase (O34453) · a predicted model of the same protein · 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 O34453
- Elsewhere: RCSB PDB 2AN2 · PDBe 2AN2 · UniProt O34453
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