MolNFT v2 · #191342 · protein
Computationally designed thioredoxin subjected to stability optimizing mutations.
7Q3K: “Computationally designed thioredoxin subjected to stability optimizing mutations.”. X-ray diffraction at 2.25, 1 ligand (SO4). MolNFT v2 #191342 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7Q3K
- Type
- protein
- Length
- 312 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.25
- Source
- synthetic construct
- Ligands
- SO4
Structure
x-ray diffraction · resolution 2.25 · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | — | protein | 104 | — | — |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Elsewhere: RCSB PDB 7Q3K · PDBe 7Q3K
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