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Crystal structure of enhancing lycopene biosynthesis protein 2
Analyse Crystal structure of enhancing lycopene biosynthesis protein 2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1VHQ
- Type
- protein
- Length
- 433 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Enhancing lycopene biosynthesis protein 2
- UniProt
- P0ABU5
- Pockets
- 4 · best druggability 0.53
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Enhancing lycopene biosynthesis protein 2 | protein | 217 | 40% helix, 18% strand | P0ABU5 |
| B | Enhancing lycopene biosynthesis protein 2 | protein | 216 | 41% helix, 18% strand | P0ABU5 |
Ligands and binding sites
- ACT · Acetate ion · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 143 | 0.53 | 0.80 | 21 | empty |
| 2 | 145 | 0.51 | 0.80 | 20 | empty |
| 3 | 50 | 0.27 | 0.74 | 14 | ACT |
| 4 | 50 | 0.26 | 0.74 | 13 | ACT |
Interfaces
1 interface between chains.
- A–B · 1573 Ų buried · 25 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 16 modified (engineered, 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 P0ABU5
- Elsewhere: RCSB PDB 1VHQ · PDBe 1VHQ · UniProt P0ABU5
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