Research workbench
Crystal structure of human GPX4 in complex with gxpep-3
Analyse Crystal structure of human GPX4 in complex with gxpep-3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5H5S
- Type
- protein
- Length
- 178 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phospholipid hydroperoxide glutathione peroxidase, mitochondrial; Gxpep-3
- EC
- 1.11.1.12
- UniProt
- P36969
Structure
x-ray diffraction · 2 distinct chains · 31% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phospholipid hydroperoxide glutathione peroxidase, mitochondrial (EC 1.11.1.12) | protein | 164 | 34% helix, 20% strand | P36969 |
| B | Gxpep-3 | protein | 14 | 0% helix, 0% strand | — |
Ligands and binding sites
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 547 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide, 1 modified (disulfide, oxidation).
Compared structures
- 5H5S · Crystal structure of human GPX4 in complex with GXpep-3 · 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 5H5S · PDBe 5H5S · UniProt P36969
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