MolNFT v2 · #152758 · protein
Structure of citryl-CoA synthetase from Hydrogenobacter thermophilus
6HXQ: “Structure of citryl-CoA synthetase from Hydrogenobacter thermophilus”. X-ray diffraction at 2.91, 1 ligand (COA). MolNFT v2 #152758 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6HXQ
- Type
- protein
- Length
- 1,504 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.91
- Source
- Hydrogenobacter thermophilus
- UniProt
- Q75VW6, Q75VW8
- Ligands
- COA
Structure
x-ray diffraction · resolution 2.91 · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | — | protein | 342 | — | Q75VW6 |
| B, D | — | protein | 410 | — | Q75VW8 |
Ligands and binding sites
- COA · Coenzyme A · ligand · 2 copies · chains A, D, B, C
- PGE · Triethylene glycol · additive · 4 copies · chains A, B, D, C
- FLC · Citrate anion · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6HXQ · Structure of citryl-CoA synthetase from hydrogenobacter thermophilus · 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 Q75VW6
- Every structure of UniProt Q75VW8
- Elsewhere: RCSB PDB 6HXQ · PDBe 6HXQ · UniProt Q75VW6 · UniProt Q75VW8
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