MolNFT v1 · #32781 · protein
Tpr domain of human PEX5P in complex with human MSCP2
2C0L · Peroxisomal targeting signal 1 receptor: “Tpr domain of human PEX5P in complex with human MSCP2”. X-ray diffraction, 2 pockets (best druggability 0.63). MolNFT v1 #32781 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2C0L
- Type
- protein
- Length
- 414 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peroxisomal targeting signal 1 receptor; Nonspecific lipid-transfer protein
- UniProt
- P50542, P22307
- Pockets
- 2 · best druggability 0.63
Structure
x-ray diffraction · 2 distinct chains · 64% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peroxisomal targeting signal 1 receptor | protein | 292 | 73% helix, 0% strand | P50542 |
| B | Nonspecific lipid-transfer protein | protein | 122 | 43% helix, 22% strand | P22307 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 207 | 0.63 | 0.83 | 26 | empty |
| 2 | 212 | 0.49 | 0.75 | 31 | empty |
Interfaces
1 interface between chains.
- A–B · 1042 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 2C0L · Tpr domain of human PEX5P in complex with human MSCP2 · the same entry in another collection · chain A against A, TM-score 1.00
- P50542 · AlphaFold monomer V2.0 prediction for peroxisomal targeting signal 1 receptor (P50542) · a predicted model of the same protein · chain A against A, TM-score 0.95
- P22307 · AlphaFold monomer V2.0 prediction for sterol carrier protein 2 (P22307) · a predicted model of the same protein · chain B against A, TM-score 0.91
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
- Every structure of UniProt P22307
- Elsewhere: RCSB PDB 2C0L · PDBe 2C0L · UniProt P50542 · UniProt P22307
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