Research workbench
Structure of a nitric oxide synthase heme protein from bacillus subtilis with tetrahydrofolate and arginine bound
Analyse Structure of a nitric oxide synthase heme protein from bacillus subtilis with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1M7V
- Type
- protein
- Length
- 361 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.95
- Source
- Bacillus subtilis
- Molecule
- Nitric Oxide Synthase
- EC
- 1.14.13.39
- UniProt
- O34453
- Ligands
- ARG, HEM, THG
- Pockets
- 3 · best druggability 0.79
Structure
x-ray diffraction · resolution 1.95 · 1 distinct chain · 44% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nitric Oxide Synthase (EC 1.14.13.39) | protein | 361 | 44% helix, 14% strand | O34453 |
Ligands and binding sites
- ARG · Arginine · ligand · chains A
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
- THG · (6S)-5,6,7,8-tetrahydrofolate · 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 | 713 | 0.79 | 0.83 | 58 | ARG, HEM |
| 2 | 96 | 0.40 | 0.77 | 14 | empty |
| 3 | 102 | 0.38 | 0.75 | 21 | empty |
Compared structures
- 1M7V · Structure of a nitric oxide synthase heme protein from bacillus subtilis with… · 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 1M7V · PDBe 1M7V · UniProt O34453
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