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Crystal structure of human glutathione peroxidase 3 (selenocysteine to glycine mutant)
Analyse Crystal structure of human glutathione peroxidase 3 (selenocysteine to glycine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2R37
- Type
- protein
- Length
- 379 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione peroxidase 3
- EC
- 1.11.1.9
- UniProt
- P22352
- Ligands
- NA, CL
- Pockets
- 1 · best druggability 0.61
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutathione peroxidase 3 (EC 1.11.1.9) | protein | 191 | 36% helix, 18% strand | P22352 |
| B | Glutathione peroxidase 3 (EC 1.11.1.9) | protein | 188 | 33% helix, 19% strand | P22352 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 444 | 0.61 | 0.76 | 37 | empty |
Interfaces
1 interface between chains.
- A–B · 238 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 2R37 · Crystal structure of human glutathione peroxidase 3 (selenocysteine to glycine mutant) · 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 P22352
- Elsewhere: RCSB PDB 2R37 · PDBe 2R37 · UniProt P22352
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