MolNFT v1 · #178037 · protein
Arabidopsis thaliana protease-associated domain of vacuolar-sorting receptor 1 in complex with cruciferin 1 C-terminal pentapeptide rvaaa (PH6.5)
7F2I: “Arabidopsis thaliana protease-associated domain of vacuolar-sorting receptor 1 in complex with cruciferin 1…”. X-ray diffraction, 1 pocket (best druggability 0.38). MolNFT v1 #178037 on GenesisL1: 3D structure, binding sites and…
- PDB
- 7F2I
- Type
- protein
- Length
- 151 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Vacuolar-sorting receptor 1; Cruciferin 1 C-terminal peptide
- UniProt
- P93026, P15455
- Pockets
- 1 · best druggability 0.38
Structure
x-ray diffraction · 2 distinct chains · 17% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Vacuolar-sorting receptor 1 | protein | 146 | 18% helix, 30% strand | P93026 |
| B | Cruciferin 1 C-terminal peptide | protein | 5 | 0% helix, 40% strand | P15455 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 84 | 0.38 | 0.76 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 314 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 7F2I · Arabidopsis thaliana protease-associated domain of vacuolar-sorting receptor 1 in complex… · the same entry in another collection · chain A against A, TM-score 1.00
- P93026 · AlphaFold monomer V2.0 prediction for vacuolar-sorting receptor 1 (P93026) · a predicted model of the same protein · chain A against A, TM-score 0.96
- P15455 · AlphaFold monomer V2.0 prediction for 12S seed storage protein CRA1 (P15455) · a predicted model of the same protein · chain B against A, TM-score 0.78
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 P93026
- Every structure of UniProt P15455
- Elsewhere: RCSB PDB 7F2I · PDBe 7F2I · UniProt P93026 · UniProt P15455
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