Research workbench
Crystal structure of the [FE3S4]-ferredoxin from the hyperthermophilic archaeon pyrococcus furiosus
Analyse Crystal structure of the [FE3S4]-ferredoxin from the hyperthermophilic archaeon… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1SIZ
- Type
- protein
- Length
- 132 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ferredoxin
- UniProt
- P29603
- Ligands
- F3S, 3CO
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Ferredoxin | protein | 66 | 27% helix, 26% strand | P29603 |
Ligands and binding sites
- F3S · FE3-S4 cluster · ligand · 2 copies · chains A, C
- 3CO · Cobalt (III) ion · metal · 4 copies · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–C · 428 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 1SIZ · Crystal structure of the [Fe3S4]-ferredoxin from the hyperthermophilic archaeon… · the same entry in another collection · chain A against A, TM-score 1.00
- P29603 · AlphaFold monomer V2.0 prediction for ferredoxin (P29603) · a predicted model of the same protein · chain C against A, TM-score 0.97
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 P29603
- Elsewhere: RCSB PDB 1SIZ · PDBe 1SIZ · UniProt P29603
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