Research workbench
Crystal structure of the conserved N-terminal domain of Pex14 from Trypanosoma brucei
Analyse Crystal structure of the conserved N-terminal domain of Pex14 from Trypanosoma… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5AON
- Type
- protein
- Length
- 244 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.646
- Source
- TRYPANOSOMA BRUCEI
- Molecule
- Peroxin 14
- UniProt
- Q8IEW2
- Ligands
- SO4
- Pockets
- 3 · best druggability 0.55
Structure
x-ray diffraction · resolution 1.646 · 2 distinct chains · 77% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Peroxin 14 | protein | 49 | 76% helix, 0% strand | Q8IEW2 |
| E | Peroxin 14 | protein | 48 | 79% helix, 0% strand | Q8IEW2 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 3 copies · chains A, D, E
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 | 183 | 0.55 | 0.79 | 27 | SO4 |
| 2 | 54 | 0.30 | 0.75 | 15 | empty |
| 3 | 51 | 0.29 | 0.75 | 15 | empty |
Interfaces
6 interfaces between chains.
- B–C · 578 Ų buried · 6 hydrogen bonds · protein-protein
- A–D · 540 Ų buried · 5 hydrogen bonds · protein-protein
- A–E · 508 Ų buried · 4 hydrogen bonds · protein-protein
- A–B · 507 Ų buried · 6 hydrogen bonds · protein-protein
- B–D · 31 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 5AON · Crystal structure of the conserved N-terminal domain of PEX14 from trypanosoma brucei · 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 Q8IEW2
- Elsewhere: RCSB PDB 5AON · PDBe 5AON · UniProt Q8IEW2
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