Research workbench
Crystal structure of the arabidopsis thaliana O-acetyl-serine-(thiol)- lyase C
Analyse Crystal structure of the arabidopsis thaliana O-acetyl-serine-(thiol)- lyase C in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4AEC
- Type
- protein
- Length
- 642 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cysteine synthase, mitochondrial
- EC
- 2.5.1.47
- UniProt
- Q43725
- Ligands
- PLP
- Pockets
- 3 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 44% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cysteine synthase, mitochondrial (EC 2.5.1.47) | protein | 323 | 44% helix, 18% strand | Q43725 |
| B | Cysteine synthase, mitochondrial (EC 2.5.1.47) | protein | 319 | 44% helix, 18% strand | Q43725 |
Ligands and binding sites
- PLP · Pyridoxal-5'-phosphate · ligand · 2 copies · chains A, B
- ACT · Acetate ion · additive · 2 copies · chains A, B
- GOL · Glycerol · additive · chains A, B
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 | 966 | 0.79 | 0.81 | 109 | PLP |
| 2 | 60 | 0.69 | 0.96 | 24 | PLP |
| 3 | 235 | 0.53 | 0.77 | 30 | empty |
Interfaces
1 interface between chains.
- A–B · 2843 Ų buried · 26 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 cofactor (pyridoxal phosphate Schiff base).
Compared structures
- 4AEC · Crystal Structure of the Arabidopsis thaliana O-Acetyl-Serine-(Thiol)- Lyase C · the same entry in another collection · chain A against A, TM-score 1.00
- Q43725 · AlphaFold monomer V2.0 prediction for cysteine synthase, mitochondrial (Q43725) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 Q43725
- Elsewhere: RCSB PDB 4AEC · PDBe 4AEC · UniProt Q43725
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