Research workbench
Chalcone synthase (G256L)
Analyse Chalcone synthase (G256L) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1I89
- Type
- protein
- Length
- 776 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chalcone synthase 2
- EC
- 2.3.1.74
- UniProt
- P30074
- Pockets
- 5 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Chalcone synthase 2 (EC 2.3.1.74) | protein | 388 | 43% helix, 21% strand | P30074 |
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 73 | 0.72 | 0.96 | 28 | empty |
| 2 | 94 | 0.67 | 0.92 | 34 | empty |
| 3 | 250 | 0.62 | 0.80 | 30 | empty |
| 4 | 206 | 0.60 | 0.81 | 30 | empty |
| 5 | 175 | 0.41 | 0.72 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 33 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (oxidation).
Compared structures
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 P30074
- Elsewhere: RCSB PDB 1I89 · PDBe 1I89 · UniProt P30074
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