Research workbench
Crystal structure of the arabidopsis exocyst subunit EXO70 family protein A1
Analyse Crystal structure of the arabidopsis exocyst subunit EXO70 family protein A1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4RL5
- Type
- protein
- Length
- 916 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Exocyst complex component EXO70A1
- UniProt
- Q9LZD3
- Pockets
- 10 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 71% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Exocyst complex component EXO70A1 | protein | 448 | 71% helix, 0% strand | Q9LZD3 |
| B | Exocyst complex component EXO70A1 | protein | 468 | 71% helix, 0% strand | Q9LZD3 |
Pockets
10 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 991 | 0.82 | 0.83 | 135 | empty |
| 2 | 429 | 0.75 | 0.84 | 66 | empty |
| 3 | 69 | 0.68 | 0.94 | 21 | empty |
| 4 | 147 | 0.63 | 0.86 | 36 | empty |
| 5 | 81 | 0.50 | 0.84 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 242 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 26 modified (engineered).
Compared structures
- 4RL5 · Crystal structure of the Arabidopsis exocyst subunit exo70 family protein A1 · the same entry in another collection · chain A against A, TM-score 1.00
- Q9LZD3 · AlphaFold monomer V2.0 prediction for exocyst complex component EXO70A1 (Q9LZD3) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 Q9LZD3
- Elsewhere: RCSB PDB 4RL5 · PDBe 4RL5 · UniProt Q9LZD3
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