Research workbench
Crystal structure at 1.25 ångströms resolution of the CYS55SER variant of the thioredoxin-like [2FE-2S] ferredoxin from aquifex aeolicus
Analyse Crystal structure at 1.25 ångströms resolution of the CYS55SER variant of the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1M2B
- Type
- protein
- Length
- 202 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- [2FE-2S] ferredoxin
- UniProt
- O66511
- Ligands
- FES
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | [2FE-2S] ferredoxin | protein | 101 | 35% helix, 22% strand | O66511 |
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 · 523 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 1M2B · Crystal structure at 1.25 Angstroms resolution of the Cys55Ser variant of the… · the same entry in another collection · chain A against A, TM-score 1.00
- O66511 · AlphaFold monomer V2.0 prediction for ferredoxin, 2FE-2S (O66511) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 O66511
- Elsewhere: RCSB PDB 1M2B · PDBe 1M2B · UniProt O66511
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