Research workbench
Serine acetyltransferase- complex with cysteine
Analyse Serine acetyltransferase- complex with cysteine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1SSQ
- Type
- protein
- Length
- 498 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Serine acetyltransferase
- EC
- 2.3.1.30
- UniProt
- P43886
- Ligands
- CYS, MG
- Pockets
- 3 · best druggability 0.36
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Serine acetyltransferase (EC 2.3.1.30) | protein | 241 | 45% helix, 15% strand | P43886 |
| D | Serine acetyltransferase (EC 2.3.1.30) | protein | 257 | 44% helix, 16% strand | P43886 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 96 | 0.36 | 0.75 | 19 | empty |
| 2 | 71 | 0.34 | 0.75 | 11 | empty |
| 3 | 55 | 0.33 | 0.77 | 17 | empty |
Interfaces
1 interface between chains.
- A–D · 472 Ų buried · 11 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 P43886
- Elsewhere: RCSB PDB 1SSQ · PDBe 1SSQ · UniProt P43886
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