Research workbench
Ensemble refinement of the protein crystal structure of thialysine N- acetyltransferase (SSAT2) from homo sapiens
Analyse Ensemble refinement of the protein crystal structure of thialysine N… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2Q4V
- Type
- protein
- Length
- 315 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Diamine acetyltransferase 2
- EC
- 2.3.1.57
- UniProt
- Q96F10
- Ligands
- ACO
- Pockets
- 3 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Diamine acetyltransferase 2 (EC 2.3.1.57) | protein | 156 | 40% helix, 31% strand | Q96F10 |
| B | Diamine acetyltransferase 2 (EC 2.3.1.57) | protein | 159 | 39% helix, 28% strand | Q96F10 |
Ligands and binding sites
- ACO · Acetyl coenzyme *A · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 572 | 0.74 | 0.81 | 50 | empty |
| 2 | 411 | 0.74 | 0.84 | 55 | ACO |
| 3 | 206 | 0.52 | 0.77 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 3351 Ų buried · 58 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (engineered).
Compared structures
- 2Q4V · Ensemble refinement of the protein crystal structure of thialysine n-acetyltransferase… · the same entry in another collection · chain A against A, TM-score 1.00
- Q96F10 · AlphaFold monomer V2.0 prediction for thialysine N-epsilon- acetyltransferase (Q96F10) · a predicted model of the same protein · chain A against A, TM-score 0.94
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 Q96F10
- Elsewhere: RCSB PDB 2Q4V · PDBe 2Q4V · UniProt Q96F10
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