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A novel conformation for the tpr domain of PEX5P
Analyse A novel conformation for the tpr domain of PEX5P in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2J9Q
- Type
- protein
- Length
- 569 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peroxisomal targeting signal 1 receptor
- UniProt
- P50542
- Ligands
- SR
- Pockets
- 6 · best druggability 0.85
Structure
x-ray diffraction · 2 distinct chains · 72% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peroxisomal targeting signal 1 receptor | protein | 300 | 71% helix, 0% strand | P50542 |
| B | Peroxisomal targeting signal 1 receptor | protein | 269 | 74% helix, 0% strand | P50542 |
Ligands and binding sites
- SR · Strontium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1002 | 0.85 | 0.86 | 98 | empty |
| 2 | 410 | 0.79 | 0.88 | 45 | empty |
| 3 | 191 | 0.50 | 0.77 | 25 | empty |
| 4 | 119 | 0.47 | 0.79 | 23 | empty |
| 5 | 55 | 0.33 | 0.77 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 1188 Ų buried · 12 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 P50542
- Elsewhere: RCSB PDB 2J9Q · PDBe 2J9Q · UniProt P50542
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