Research workbench
Crystal structure of a mammalian 2-cys peroxiredoxin, HBP23.
Analyse Crystal structure of a mammalian 2-cys peroxiredoxin, HBP23. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1QQ2
- Type
- protein
- Length
- 346 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thioredoxin peroxidase 2
- UniProt
- Q63716
- Ligands
- CL
- Pockets
- 3 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Thioredoxin peroxidase 2 | protein | 173 | 27% helix, 25% strand | Q63716 |
Ligands and binding sites
- CL · Chloride ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 105 | 0.78 | 0.98 | 28 | empty |
| 2 | 160 | 0.45 | 0.75 | 35 | CL |
| 3 | 157 | 0.44 | 0.75 | 30 | CL |
Interfaces
1 interface between chains.
- A–B · 1305 Ų buried · 16 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
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 Q63716
- Elsewhere: RCSB PDB 1QQ2 · PDBe 1QQ2 · UniProt Q63716
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