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 v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phospholipid hydroperoxide glutathione peroxidase
- EC
- 1.11.1.12
- UniProt
- P36969
- Ligands
- CL
Structure
x-ray diffraction · 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
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