Research workbench
O-acetylserine sulfhydrylase complex
Analyse O-acetylserine sulfhydrylase complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1Y7L
- Type
- protein
- Length
- 314 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- O-acetylserine sulfhydrylase; Decamer fragment of serine acetyltransferase
- EC
- 2.5.1.47
- UniProt
- P45040, P43886
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.65
Structure
x-ray diffraction · 2 distinct chains · 42% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | O-acetylserine sulfhydrylase (EC 2.5.1.47) | protein | 310 | 43% helix, 17% strand | P45040 |
| P | Decamer fragment of serine acetyltransferase | protein | 4 | 0% helix, 0% strand | P43886 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 370 | 0.65 | 0.80 | 37 | empty |
| 2 | 123 | 0.48 | 0.79 | 15 | empty |
Interfaces
1 interface between chains.
- A–P · 491 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (cofactor).
Compared structures
- 1Y7L · O-Acetylserine Sulfhydrylase Complex · the same entry in another collection · chain A against A, TM-score 1.00
- P45040 · AlphaFold monomer V2.0 prediction for cysteine synthase (P45040) · a predicted model of the same protein · chain A against A, TM-score 0.98
- P43886 · AlphaFold monomer V2.0 prediction for serine acetyltransferase (P43886) · a predicted model of the same protein · chain P against A, TM-score 0.78
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 P45040
- Every structure of UniProt P43886
- Elsewhere: RCSB PDB 1Y7L · PDBe 1Y7L · UniProt P45040 · UniProt P43886
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