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The crystal structure of type II dehydroquinase from butyrivibrio crossotus dsm 2876
Analyse The crystal structure of type II dehydroquinase from butyrivibrio crossotus dsm… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6HS8
- Type
- protein
- Length
- 144 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 3-dehydroquinate dehydratase
- EC
- 4.2.1.10
- UniProt
- D4S0D1
- Ligands
- PO4
- Pockets
- 1 · best druggability 0.50
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 3-dehydroquinate dehydratase (EC 4.2.1.10) | protein | 144 | 46% helix, 21% strand | D4S0D1 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · chains A
- TLA · L(+)-tartaric acid · additive · 3 copies · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 92 | 0.50 | 0.83 | 20 | TLA, GOL |
Compared structures
- 6HS8 · The crystal structure of type II Dehydroquinase from Butyrivibrio crossotus DSM 2876 · the same entry in another collection · chain A against A, TM-score 1.00
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 D4S0D1
- Elsewhere: RCSB PDB 6HS8 · PDBe 6HS8 · UniProt D4S0D1
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