Research workbench
Structure of citryl-CoA lyase from hydrogenobacter thermophilus
Analyse Structure of citryl-CoA lyase from hydrogenobacter thermophilus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6HXP
- Type
- protein
- Length
- 256 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Citryl-CoA lyase
- UniProt
- Q75VX1
- Ligands
- COA, SO4
- Pockets
- 2 · best druggability 0.46
Structure
x-ray diffraction · 1 distinct chain · 57% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Citryl-CoA lyase | protein | 256 | 57% helix, 5% strand | Q75VX1 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 156 | 0.46 | 0.76 | 28 | empty |
| 2 | 74 | 0.33 | 0.75 | 14 | empty |
Compared structures
- 6HXP · Structure of citryl-CoA lyase 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 Q75VX1
- Elsewhere: RCSB PDB 6HXP · PDBe 6HXP · UniProt Q75VX1
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