Research workbench
Complex between 4-hydroxybutyrate CoA-transferase from clostridium aminobutyricum and CoA
Analyse Complex between 4-hydroxybutyrate CoA-transferase from clostridium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3QDQ
- Type
- protein
- Length
- 447 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 4-hydroxybutyrate CoA-transferase
- EC
- 2.8.3.-
- UniProt
- Q9RM86
- Ligands
- COA
- Pockets
- 1 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 4-hydroxybutyrate CoA-transferase (EC 2.8.3.-) | protein | 447 | 30% helix, 22% strand | Q9RM86 |
Ligands and binding sites
- COA · Coenzyme A · ligand · 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 | 473 | 0.70 | 0.80 | 69 | COA |
Compared structures
- 3QDQ · Complex between 4-hydroxybutyrate CoA-transferase from Clostridium aminobutyricum and CoA · 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 Q9RM86
- Elsewhere: RCSB PDB 3QDQ · PDBe 3QDQ · UniProt Q9RM86
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