Research workbench
Archaeal dehydroquinase
Analyse Archaeal dehydroquinase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2OX1
- Type
- protein
- Length
- 784 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 3-dehydroquinate dehydratase
- EC
- 4.2.1.10
- UniProt
- O30011
- Pockets
- 5 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | 3-dehydroquinate dehydratase (EC 4.2.1.10) | protein | 196 | 36% helix, 26% strand | O30011 |
Ligands and binding sites
- GOL · Glycerol · additive · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 193 | 0.69 | 0.87 | 31 | GOL |
| 2 | 168 | 0.67 | 0.87 | 31 | GOL |
| 3 | 175 | 0.65 | 0.85 | 26 | GOL |
| 4 | 171 | 0.64 | 0.85 | 31 | GOL |
| 5 | 214 | 0.50 | 0.76 | 43 | empty |
Interfaces
3 interfaces between chains.
- C–D · 1142 Ų buried · 7 hydrogen bonds · protein-protein
- A–B · 1111 Ų buried · 6 hydrogen bonds · protein-protein
- B–C · 577 Ų buried · 11 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 O30011
- Elsewhere: RCSB PDB 2OX1 · PDBe 2OX1 · UniProt O30011
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