MolNFT v1 · #60567 · protein
Structure of peroxisomal targeting signal 1 (PTS1) binding domain of trypanosoma brucei peroxin 5 (TBPEX5)COMPLEXED to T. brucei phosphofructokinase (pfk) PTS1 peptide
3CVL · Peroxisome targeting signal 1 receptor PEX5: “Structure of peroxisomal targeting signal 1 (PTS1) binding domain of trypanosoma brucei peroxin 5…”. X-ray diffraction, 4 pockets (best druggability 0.60). MolNFT v1 #60567 on GenesisL1…
- PDB
- 3CVL
- Type
- protein
- Length
- 299 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peroxisome targeting signal 1 receptor PEX5; T. brucei pfk PTS1 peptide ac-heelakl
- UniProt
- Q9U7C3, O15648
- Pockets
- 4 · best druggability 0.60
Structure
x-ray diffraction · 2 distinct chains · 71% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peroxisome targeting signal 1 receptor PEX5 | protein | 294 | 72% helix, 0% strand | Q9U7C3 |
| B | T. brucei pfk PTS1 peptide ac-heelakl | protein | 5 | 0% helix, 0% strand | O15648 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 213 | 0.60 | 0.81 | 35 | empty |
| 2 | 65 | 0.53 | 0.87 | 28 | empty |
| 3 | 64 | 0.41 | 0.81 | 17 | empty |
| 4 | 84 | 0.34 | 0.74 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 577 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 3CVL · Structure of Peroxisomal Targeting Signal 1 (PTS1) binding domain of Trypanosoma brucei… · the same entry in another collection · chain A against A, TM-score 1.00
- O15648 · AlphaFold monomer V2.0 prediction for ATP-dependent 6-phosphofructokinase (O15648) · a predicted model of the same protein · chain B against A, TM-score 0.70
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 Q9U7C3
- Every structure of UniProt O15648
- Elsewhere: RCSB PDB 3CVL · PDBe 3CVL · UniProt Q9U7C3 · UniProt O15648
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