Research workbench
Apo form of the tpr domain of the PEX5P receptor
Analyse Apo form of the tpr domain of the PEX5P receptor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2C0M
- Type
- protein
- Length
- 1,198 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peroxisomal targeting signal 1 receptor
- UniProt
- P50542
- Pockets
- 12 · best druggability 0.81
Structure
x-ray diffraction · 2 distinct chains · 69% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Peroxisomal targeting signal 1 receptor | protein | 297 | 70% helix, 0% strand | P50542 |
| C, F | Peroxisomal targeting signal 1 receptor | protein | 302 | 69% helix, 0% strand | P50542 |
Pockets
12 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 890 | 0.81 | 0.83 | 83 | empty |
| 2 | 1053 | 0.78 | 0.80 | 83 | empty |
| 3 | 954 | 0.72 | 0.76 | 85 | empty |
| 4 | 261 | 0.63 | 0.81 | 45 | empty |
| 5 | 290 | 0.62 | 0.80 | 28 | empty |
Interfaces
5 interfaces between chains.
- B–C · 923 Ų buried · 12 hydrogen bonds · protein-protein
- A–C · 537 Ų buried · 8 hydrogen bonds · protein-protein
- C–F · 413 Ų buried · 4 hydrogen bonds · protein-protein
- A–B · 335 Ų buried · 8 hydrogen bonds · protein-protein
- B–F · 31 Ų buried · 1 hydrogen bond · 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 2C0M · PDBe 2C0M · UniProt P50542
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