Research workbench
1.45 a resolution structure of the C-terminally truncated [2FE-2S] ferredoxin (bfd) R26E/K46Y mutant from pseudomonas aeruginosa
Analyse 1.45 a resolution structure of the C-terminally truncated [2FE-2S] ferredoxin… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6E6S
- Type
- protein
- Length
- 112 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bacterioferritin-associated ferredoxin
- UniProt
- A0A069Q647
- Ligands
- FES
Structure
x-ray diffraction · 1 distinct chain · 54% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Bacterioferritin-associated ferredoxin | protein | 56 | 54% helix, 9% strand | A0A069Q647 |
Ligands and binding sites
- FES · Fe2/s2 (inorganic) cluster · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 438 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 6E6S · 1.45 A resolution structure of the C-terminally truncated [2Fe-2S] ferredoxin (Bfd)… · 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 A0A069Q647
- Elsewhere: RCSB PDB 6E6S · PDBe 6E6S · UniProt A0A069Q647
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