Research workbench
Structure of reduced C73S/C85S putidaredoxin, a [2FE-2S] ferredoxin from pseudomonas putida
Analyse Structure of reduced C73S/C85S putidaredoxin, a [2FE-2S] ferredoxin from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1XLO
- Type
- protein
- Length
- 212 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putidaredoxin
- EC
- 1.9.3.2
- UniProt
- P00259
- Ligands
- FES
Structure
x-ray diffraction · 1 distinct chain · 18% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Putidaredoxin (EC 1.9.3.2) | protein | 106 | 18% helix, 22% strand | P00259 |
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 · 357 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 1XLO · Structure of reduced C73S/C85S putidaredoxin, a [2Fe-2S] ferredoxin from Pseudomonas… · the same entry in another collection · chain A against A, TM-score 1.00
- P00259 · AlphaFold monomer V2.0 prediction for putidaredoxin (P00259) · 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 P00259
- Elsewhere: RCSB PDB 1XLO · PDBe 1XLO · UniProt P00259
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