Research workbench
NMR study of reduced high potential iron sulfur protein
Analyse NMR study of reduced high potential iron sulfur protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1NOE
- Type
- protein
- Length
- 86 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- High potential iron sulfur protein
- UniProt
- P00260
- Ligands
- SF4
Structure
solution nmr · 1 distinct chain · 19% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | High potential iron sulfur protein | protein | 86 | 19% helix, 20% strand | P00260 |
Ligands and binding sites
- SF4 · Iron/sulfur cluster · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1NOE · NMR study of reduced high potential iron sulfur protein · the same entry in another collection · chain A against A, TM-score 1.00
- P00260 · AlphaFold monomer V2.0 prediction for high-potential iron-sulfur protein (P00260) · a predicted model of the same protein · chain A against A, TM-score 0.91
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 P00260
- Elsewhere: RCSB PDB 1NOE · PDBe 1NOE · UniProt P00260
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