Research workbench
Crystal structure of O-acetylserine sulfhydrylase from arabidopsis thaliana in complex with C-terminal peptide from arabidopsis serine acetyltransferase
Analyse Crystal structure of O-acetylserine sulfhydrylase from arabidopsis thaliana in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ISQ
- Type
- protein
- Length
- 328 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cysteine synthase; Serine acetyltransferase 1
- EC
- 2.5.1.47, 2.3.1.30
- UniProt
- P47998, Q42588
- Ligands
- PLP, SO4
- Pockets
- 3 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cysteine synthase (EC 2.5.1.47) | protein | 320 | 46% helix, 18% strand | P47998 |
| B | Serine acetyltransferase 1 (EC 2.3.1.30) | protein | 8 | 0% helix, 0% strand | Q42588 |
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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 70 | 0.74 | 0.98 | 27 | PLP |
| 2 | 83 | 0.41 | 0.78 | 21 | SO4 |
| 3 | 54 | 0.36 | 0.79 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 660 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 cofactor (pyridoxal phosphate Schiff base).
Compared structures
- 2ISQ · Crystal Structure of O-Acetylserine Sulfhydrylase from Arabidopsis Thaliana in Complex… · the same entry in another collection · chain A against A, TM-score 1.00
- P47998 · AlphaFold monomer V2.0 prediction for cysteine synthase 1 (P47998) · a predicted model of the same protein · chain A against A, TM-score 0.99
- Q42588 · AlphaFold monomer V2.0 prediction for serine acetyltransferase 1, chloroplastic (Q42588) · a predicted model of the same protein · chain B against A, TM-score 0.35
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 P47998
- Every structure of UniProt Q42588
- Elsewhere: RCSB PDB 2ISQ · PDBe 2ISQ · UniProt P47998 · UniProt Q42588
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