MolNFT v1 · #151590 · protein
The crystal structure of type II dehydroquinase from butyrivibrio crossotus dsm 2876
6HSA · 3-dehydroquinate dehydratase: “The crystal structure of type II dehydroquinase from butyrivibrio crossotus dsm 2876”. X-ray diffraction, 3 ligands (ETE, SER, SO4). MolNFT v1 #151590 on GenesisL1: 3D structure, binding sites and…
- PDB
- 6HSA
- Type
- protein
- Length
- 145 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
- ETE, SER, SO4
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 3-dehydroquinate dehydratase (EC 4.2.1.10) | protein | 145 | 46% helix, 19% strand | D4S0D1 |
Ligands and binding sites
- ETE · 2-{2-[2-2-(methoxy-ethoxy)-ethoxy]-ethoxy}-ethanol · ligand · chains A
- SER · Serine · ligand · chains A
- SO4 · Sulfate ion · ion · 2 copies · chains A
- FLC · Citrate anion · additive · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 6HSA · 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 6HSA · PDBe 6HSA · UniProt D4S0D1
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