Research workbench
I40N mutant of azotobacter vinelandii fdi
Analyse I40N mutant of azotobacter vinelandii fdi in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1B0V
- Type
- protein
- Length
- 424 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (ferredoxin)
- UniProt
- P00214
- Ligands
- SF4, F3S
- Pockets
- 1 · best druggability 0.28
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Protein (ferredoxin) | protein | 106 | 33% helix, 15% strand | P00214 |
Ligands and binding sites
- SF4 · Iron/sulfur cluster · ligand · 4 copies · chains A, B, C, D
- F3S · FE3-S4 cluster · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 65 | 0.28 | 0.73 | 22 | empty |
Interfaces
3 interfaces between chains.
- A–B · 436 Ų buried · 6 hydrogen bonds · protein-protein
- C–D · 424 Ų buried · 6 hydrogen bonds · protein-protein
- B–D · 379 Ų buried · 2 hydrogen bonds · protein-protein
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 P00214
- Elsewhere: RCSB PDB 1B0V · PDBe 1B0V · UniProt P00214
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