Research workbench
Crystal structure of the 3-dehydroquinate dehydratase from aquifex aeolicus VF5
Analyse Crystal structure of the 3-dehydroquinate dehydratase from aquifex aeolicus VF5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2EGZ
- Type
- protein
- Length
- 434 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 3-dehydroquinate dehydratase
- EC
- 4.2.1.10
- UniProt
- O66440
- Pockets
- 2 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 46% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 3-dehydroquinate dehydratase (EC 4.2.1.10) | protein | 216 | 45% helix, 22% strand | O66440 |
| C | 3-dehydroquinate dehydratase (EC 4.2.1.10) | protein | 218 | 47% helix, 22% strand | O66440 |
Ligands and binding sites
- TLA · L(+)-tartaric acid · additive · 2 copies · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 739 | 0.70 | 0.77 | 55 | TLA |
| 2 | 225 | 0.55 | 0.78 | 30 | TLA |
Interfaces
1 interface between chains.
- A–C · 323 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 2EGZ · Crystal structure of the 3-dehydroquinate dehydratase from Aquifex aeolicus VF5 · the same entry in another collection · chain A against A, TM-score 1.00
- O66440 · AlphaFold monomer V2.0 prediction for 3-dehydroquinate dehydratase (O66440) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 O66440
- Elsewhere: RCSB PDB 2EGZ · PDBe 2EGZ · UniProt O66440
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.