Research workbench
Heme-no complex in a bacterial nitric oxide synthase
Analyse Heme-no complex in a bacterial 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
- 2FBZ
- Type
- protein
- Length
- 361 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nitric oxide synthase oxygenase
- UniProt
- O34453
- Ligands
- HEM, H2B, HAR, NO
- Pockets
- 3 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| X | Nitric oxide synthase oxygenase | protein | 361 | 42% helix, 14% strand | O34453 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · chains X
- H2B · 2-amino-6-(1,2-dihydroxy-propyl)-7,8-dihydro-6H-pteridin-4-one · ligand · chains X
- HAR · N-omega-hydroxy-L-arginine · ligand · chains X
- NO · Nitric oxide · ion · chains X
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 | 695 | 0.78 | 0.83 | 59 | HEM, H2B, NO, HAR |
| 2 | 112 | 0.42 | 0.77 | 21 | empty |
| 3 | 97 | 0.40 | 0.77 | 17 | empty |
Compared structures
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 2FBZ · PDBe 2FBZ · UniProt O34453
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