Research workbench
Crystal structure of the 2[4FE-4S] ferredoxin from escherichia COLI
Analyse Crystal structure of the 2[4FE-4S] ferredoxin from escherichia COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ZVS
- Type
- protein
- Length
- 241 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uncharacterized ferredoxin-like protein yfhl
- UniProt
- P52102
- Ligands
- SF4
- Pockets
- 1 · best druggability 0.42
Structure
x-ray diffraction · 2 distinct chains · 25% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized ferredoxin-like protein yfhl | protein | 81 | 25% helix, 12% strand | P52102 |
| B, C | Uncharacterized ferredoxin-like protein yfhl | protein | 80 | 25% helix, 13% strand | P52102 |
Ligands and binding sites
- SF4 · Iron/sulfur cluster · ligand · 6 copies · chains A, B, C
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 | 169 | 0.42 | 0.73 | 29 | empty |
Interfaces
3 interfaces between chains.
- B–C · 288 Ų buried · 3 hydrogen bonds · protein-protein
- A–C · 127 Ų buried · 0 hydrogen bonds · protein-protein
- A–B · 11 Ų buried · 0 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 P52102
- Elsewhere: RCSB PDB 2ZVS · PDBe 2ZVS · UniProt P52102
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