Research workbench
Chalcone isomerase and naringenin
Analyse Chalcone isomerase and naringenin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1EYQ
- Type
- protein
- Length
- 424 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chalcone-flavonone isomerase 1
- EC
- 5.5.1.6
- UniProt
- P28012
- Ligands
- NAR, SO4
- Pockets
- 3 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Chalcone-flavonone isomerase 1 (EC 5.5.1.6) | protein | 212 | 39% helix, 31% strand | P28012 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 611 | 0.84 | 0.89 | 79 | SO4, NAR |
| 2 | 256 | 0.64 | 0.82 | 29 | SO4, NAR |
| 3 | 57 | 0.26 | 0.72 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 948 Ų buried · 10 hydrogen bonds · protein-protein
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 P28012
- Elsewhere: RCSB PDB 1EYQ · PDBe 1EYQ · UniProt P28012
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