Research workbench
Replacement for 1FDX 2(4FE4S) ferredoxin from (now) peptostreptococcus asaccharolyticus
Analyse Replacement for 1FDX 2(4FE4S) ferredoxin from (now) peptostreptococcus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1DUR
- Type
- protein
- Length
- 55 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 2[4FE-4S] ferredoxin
- UniProt
- P00193
- Ligands
- SF4
Structure
x-ray diffraction · 1 distinct chain · 15% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 2[4FE-4S] ferredoxin | protein | 55 | 15% helix, 18% strand | P00193 |
Ligands and binding sites
- SF4 · Iron/sulfur cluster · ligand · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1DUR · Replacement for 1FDX 2(4FE4S) ferredoxin from (NOW) Peptostreptococcus asaccharolyticus · the same entry in another collection · chain A against A, TM-score 1.00
- P00193 · AlphaFold monomer V2.0 prediction for ferredoxin (P00193) · a predicted model of the same protein · chain A against A, TM-score 0.93
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 P00193
- Elsewhere: RCSB PDB 1DUR · PDBe 1DUR · UniProt P00193
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