Research workbench
Human peroxiredoxin 5 with a fragment
Analyse Human peroxiredoxin 5 with a fragment in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4K7N
- Type
- protein
- Length
- 483 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peroxiredoxin-5, mitochondrial
- EC
- 1.11.1.15
- UniProt
- P30044
- Ligands
- MCT
- Pockets
- 4 · best druggability 0.44
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Peroxiredoxin-5, mitochondrial (EC 1.11.1.15) | protein | 161 | 32% helix, 25% strand | P30044 |
Ligands and binding sites
- MCT · 4-methylcatechol · ligand · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 93 | 0.44 | 0.79 | 18 | MCT |
| 2 | 114 | 0.40 | 0.76 | 24 | empty |
| 3 | 91 | 0.37 | 0.76 | 20 | empty |
| 4 | 67 | 0.30 | 0.74 | 14 | empty |
Interfaces
2 interfaces between chains.
- B–C · 799 Ų buried · 2 hydrogen bonds · protein-protein
- A–B · 430 Ų buried · 7 hydrogen bonds · protein-protein
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 P30044
- Elsewhere: RCSB PDB 4K7N · PDBe 4K7N · UniProt P30044
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