MolNFT v1 · #46111 · protein
Soluble domain of the rieske iron-sulfur protein from rhodobacter sphaeroides
2NUK · Ubiquinol-cytochrome C reductase iron-sulfur subunit: “Soluble domain of the rieske iron-sulfur protein from rhodobacter sphaeroides”. X-ray diffraction, 1 ligand (FES). MolNFT v1 #46111 on GenesisL1: 3D structure, binding sites and…
- PDB
- 2NUK
- Type
- protein
- Length
- 141 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ubiquinol-cytochrome C reductase iron-sulfur subunit
- EC
- 1.10.2.2
- UniProt
- Q02762
- Ligands
- FES
Structure
x-ray diffraction · 1 distinct chain · 11% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ubiquinol-cytochrome C reductase iron-sulfur subunit (EC 1.10.2.2) | protein | 141 | 11% helix, 35% strand | Q02762 |
Ligands and binding sites
- FES · Fe2/s2 (inorganic) cluster · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 2NUK · Soluble Domain of the Rieske Iron-Sulfur Protein from Rhodobacter sphaeroides · the same entry in another collection · chain A against A, TM-score 1.00
- Q02762 · AlphaFold monomer V2.0 prediction for ubiquinol-cytochrome C reductase iron-sulfur… · 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 Q02762
- Elsewhere: RCSB PDB 2NUK · PDBe 2NUK · UniProt Q02762
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