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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
- 6HS9
- Type
- protein
- Length
- 145 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.05
- Source
- Butyrivibrio crossotus DSM 2876
- Molecule
- 3-dehydroquinate dehydratase
- EC
- 4.2.1.10
- UniProt
- D4S0D1
- Ligands
- 3DS
Structure
x-ray diffraction · resolution 1.05 · 1 distinct chain · 47% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 3-dehydroquinate dehydratase (EC 4.2.1.10) | protein | 145 | 47% helix, 19% strand | D4S0D1 |
Ligands and binding sites
- 3DS · (4S,5R)-4,5-dihydroxy-3-oxocyclohex-1-ene-1-carboxylic acid · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6HS9 · 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 6HS9 · PDBe 6HS9 · UniProt D4S0D1
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