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Structural and Mechanistic Insights into CO2 Activation by Nitrogenase Iron Protein
Analyse Structural and Mechanistic Insights into CO2 Activation by Nitrogenase Iron… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6O0B
- Type
- protein
- Length
- 572 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.6
- Source
- Azotobacter vinelandii (strain DJ / ATCC BAA-1303)
- Molecule
- Nitrogenase iron protein
- EC
- 1.18.6.1
- UniProt
- C1DGZ6
- Ligands
- SF4
- Pockets
- 4 · best druggability 0.81
Structure
x-ray diffraction · resolution 1.6 · 2 distinct chains · 41% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nitrogenase iron protein (EC 1.18.6.1) | protein | 285 | 41% helix, 16% strand | C1DGZ6 |
| B | Nitrogenase iron protein (EC 1.18.6.1) | protein | 287 | 42% helix, 16% strand | C1DGZ6 |
Ligands and binding sites
- SF4 · Iron/sulfur cluster · ligand · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 875 | 0.81 | 0.83 | 113 | SF4 |
| 2 | 82 | 0.42 | 0.79 | 15 | empty |
| 3 | 70 | 0.37 | 0.78 | 16 | empty |
| 4 | 77 | 0.36 | 0.77 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 1494 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 6O0B · Structural and mechanistic insights into CO2 activation by nitrogenase iron protein · 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 C1DGZ6
- Elsewhere: RCSB PDB 6O0B · PDBe 6O0B · UniProt C1DGZ6
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