Research workbench
Succinyl-COA:ACETATE CoA-transferase (AARCH6-E294A) in complex with CoA
Analyse Succinyl-COA:ACETATE CoA-transferase (AARCH6-E294A) in complex with CoA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4EUB
- Type
- protein
- Length
- 1,008 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Succinyl-COA:ACETATE coenzyme a transferase
- EC
- 2.8.3.18
- UniProt
- B3EY95
- Ligands
- COA, CL
- Pockets
- 7 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Succinyl-COA:ACETATE coenzyme a transferase (EC 2.8.3.18) | protein | 504 | 34% helix, 21% strand | B3EY95 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 174 | 0.80 | 0.96 | 41 | CL |
| 2 | 65 | 0.73 | 0.98 | 23 | empty |
| 3 | 574 | 0.71 | 0.80 | 76 | COA |
| 4 | 540 | 0.71 | 0.80 | 76 | COA |
| 5 | 57 | 0.33 | 0.77 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 3589 Ų buried · 49 hydrogen bonds · protein-protein
Compared structures
- 4EUB · Succinyl-CoA:acetate CoA-transferase (AarCH6-E294A) in complex with CoA · the same entry in another collection · chain A against A, TM-score 1.00
- B3EY95 · AlphaFold monomer V2.0 prediction for succinyl-COA:ACETATE CoA- transferase (B3EY95) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 B3EY95
- Elsewhere: RCSB PDB 4EUB · PDBe 4EUB · UniProt B3EY95
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