Research workbench
Acetyl-CoA synthetase, R194A mutation
Analyse Acetyl-CoA synthetase, R194A mutation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2P2M
- Type
- protein
- Length
- 1,271 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetyl-coenzyme a synthetase
- EC
- 6.2.1.1
- UniProt
- Q8ZKF6
- Ligands
- PRX
- Pockets
- 11 · best druggability 0.83
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acetyl-coenzyme a synthetase (EC 6.2.1.1) | protein | 638 | 34% helix, 26% strand | Q8ZKF6 |
| B | Acetyl-coenzyme a synthetase (EC 6.2.1.1) | protein | 633 | 34% helix, 25% strand | Q8ZKF6 |
Ligands and binding sites
- PRX · Adenosine-5'-monophosphate-propyl ester · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1001 | 0.83 | 0.84 | 115 | PRX |
| 2 | 1192 | 0.79 | 0.81 | 126 | PRX |
| 3 | 117 | 0.55 | 0.83 | 16 | empty |
| 4 | 100 | 0.52 | 0.83 | 25 | empty |
| 5 | 98 | 0.51 | 0.82 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 674 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
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 Q8ZKF6
- Elsewhere: RCSB PDB 2P2M · PDBe 2P2M · UniProt Q8ZKF6
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