Research workbench
Crystal structure of serine acetyltransferase from salmonella typhimurium complexed with cysteine
Analyse Crystal structure of serine acetyltransferase from salmonella typhimurium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7E3Y
- Type
- protein
- Length
- 771 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Serine acetyltransferase
- EC
- 2.3.1.30
- UniProt
- A0A0D6I3Y9
- Ligands
- CYS
- Pockets
- 6 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Serine acetyltransferase (EC 2.3.1.30) | protein | 257 | 44% helix, 14% strand | A0A0D6I3Y9 |
Ligands and binding sites
- CYS · Cysteine · ligand · 3 copies · chains A, C, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 221 | 0.77 | 0.91 | 55 | CYS |
| 2 | 244 | 0.77 | 0.90 | 58 | CYS |
| 3 | 239 | 0.77 | 0.90 | 57 | CYS |
| 4 | 897 | 0.76 | 0.79 | 77 | empty |
| 5 | 55 | 0.29 | 0.75 | 13 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1401 Ų buried · 9 hydrogen bonds · protein-protein
- B–C · 1397 Ų buried · 10 hydrogen bonds · protein-protein
- A–C · 1389 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 7E3Y · Crystal structure of serine acetyltransferase from Salmonella typhimurium complexed with… · 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 A0A0D6I3Y9
- Elsewhere: RCSB PDB 7E3Y · PDBe 7E3Y · UniProt A0A0D6I3Y9
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