MolNFT v1 · #106610 · protein
Crystal structure of protease-associated domain of arabidopsis VSR1 in complex with aleurain peptide
4TJX · Vacuolar-sorting receptor 1: “Crystal structure of protease-associated domain of arabidopsis VSR1 in complex with aleurain peptide”. X-ray diffraction, 1 pocket (best druggability 0.31). MolNFT v1 #106610 on GenesisL1: 3D structure…
- PDB
- 4TJX
- Type
- protein
- Length
- 156 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Vacuolar-sorting receptor 1; Aleurain peptide
- UniProt
- P93026
- Pockets
- 1 · best druggability 0.31
Structure
x-ray diffraction · 2 distinct chains · 20% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Vacuolar-sorting receptor 1 | protein | 153 | 20% helix, 28% strand | P93026 |
| B | Aleurain peptide | protein | 3 | 0% helix, 0% strand | — |
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 | 55 | 0.31 | 0.76 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 229 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 4TJX · Crystal structure of protease-associated domain of Arabidopsis VSR1 in complex with… · 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
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
- Elsewhere: RCSB PDB 4TJX · PDBe 4TJX · UniProt P93026
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