Research workbench
Crystal structure of the selenocysteine to cysteine mutant of human glutathionine peroxidase 2 (GPX2)
Analyse Crystal structure of the selenocysteine to cysteine mutant of human… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2HE3
- Type
- protein
- Length
- 185 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione peroxidase 2
- EC
- 1.11.1.9
- UniProt
- P18283
- Ligands
- CL
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutathione peroxidase 2 (EC 1.11.1.9) | protein | 185 | 30% helix, 20% strand | P18283 |
Ligands and binding sites
- CL · Chloride ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2HE3 · Crystal structure of the selenocysteine to cysteine mutant of human glutathionine… · 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 P18283
- Elsewhere: RCSB PDB 2HE3 · PDBe 2HE3 · UniProt P18283
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