Research workbench
wildtype form (apo) of human GPX4 with Se-Cys46
Analyse wildtype form (apo) of human GPX4 with Se-Cys46 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6HN3
- Type
- protein
- Length
- 167 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.01
- Source
- Homo sapiens
- Molecule
- Phospholipid hydroperoxide glutathione peroxidase
- EC
- 1.11.1.12
- UniProt
- P36969
- Ligands
- CL
Structure
x-ray diffraction · resolution 1.01 · 1 distinct chain · 33% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phospholipid hydroperoxide glutathione peroxidase (EC 1.11.1.12) | protein | 167 | 33% helix, 21% strand | P36969 |
Ligands and binding sites
- CL · Chloride ion · ion · 2 copies · chains A
- EOH · Ethanol · additive · 2 copies · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6HN3 · Wildtype form (apo) of human GPX4 with se-CYS46 · the same entry in another collection · chain A against A, TM-score 1.00
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 P36969
- Elsewhere: RCSB PDB 6HN3 · PDBe 6HN3 · UniProt P36969
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.