Research workbench
Structure of the [2FE-2S] ferredoxin I from the blue-green alga aphanothece sacrum at 2.2 ångströms resolution
Analyse Structure of the [2FE-2S] ferredoxin I from the blue-green alga aphanothece… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1FXI
- Type
- protein
- Length
- 384 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ferredoxin I
- UniProt
- P00250
- Ligands
- FES
- Pockets
- 2 · best druggability 0.61
Structure
x-ray diffraction · 1 distinct chain · 11% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Ferredoxin I | protein | 96 | 11% helix, 30% strand | P00250 |
Ligands and binding sites
- FES · Fe2/s2 (inorganic) 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
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 437 | 0.61 | 0.76 | 41 | empty |
| 2 | 92 | 0.38 | 0.76 | 24 | empty |
Interfaces
4 interfaces between chains.
- A–D · 406 Ų buried · 6 hydrogen bonds · protein-protein
- A–C · 84 Ų buried · 1 hydrogen bond · protein-protein
- C–D · 44 Ų buried · 0 hydrogen bonds · protein-protein
- B–C · 26 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 1FXI · Structure of the [2FE-2S] ferredoxin I from the blue-green alga aphanothece sacrum at 2.2… · the same entry in another collection · chain D against D, TM-score 1.00
- P00250 · AlphaFold monomer V2.0 prediction for ferredoxin-1 (P00250) · a predicted model of the same protein · chain B against A, TM-score 0.94
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 P00250
- Elsewhere: RCSB PDB 1FXI · PDBe 1FXI · UniProt P00250
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