Research workbench
Crystal structure of peroxiredoxin asp F3 C31S/C61S variant
Analyse Crystal structure of peroxiredoxin asp F3 C31S/C61S variant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5J9C
- Type
- protein
- Length
- 337 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peroxiredoxin asp F3
- EC
- 1.11.1.15
- UniProt
- O43099
- Ligands
- MG
- Pockets
- 1 · best druggability 0.55
Structure
x-ray diffraction · 2 distinct chains · 31% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peroxiredoxin asp F3 (EC 1.11.1.15) | protein | 167 | 30% helix, 24% strand | O43099 |
| B | Peroxiredoxin asp F3 (EC 1.11.1.15) | protein | 170 | 31% helix, 24% strand | O43099 |
Ligands and binding sites
- MG · Magnesium ion · metal · chains A
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 | 288 | 0.55 | 0.76 | 39 | empty |
Interfaces
1 interface between chains.
- A–B · 750 Ų buried · 9 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 O43099
- Elsewhere: RCSB PDB 5J9C · PDBe 5J9C · UniProt O43099
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