Research workbench
Crystal structure of the cystine C-S lyase C-des
Analyse Crystal structure of the cystine C-S lyase C-des in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ELQ
- Type
- protein
- Length
- 762 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- L-CYSTEINE/L-cystine C-S lyase
- UniProt
- Q9ZHG9
- Ligands
- PLP, K
- Pockets
- 5 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | L-CYSTEINE/L-cystine C-S lyase | protein | 381 | 41% helix, 18% strand | Q9ZHG9 |
Ligands and binding sites
- PLP · Pyridoxal-5'-phosphate · ligand · 2 copies · chains A, B
- K · Potassium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 138 | 0.80 | 0.98 | 31 | empty |
| 2 | 557 | 0.73 | 0.81 | 66 | PLP |
| 3 | 570 | 0.71 | 0.79 | 63 | PLP |
| 4 | 62 | 0.48 | 0.85 | 18 | empty |
| 5 | 66 | 0.43 | 0.81 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 3032 Ų buried · 43 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 cofactor (pyridoxal phosphate Schiff base).
Compared structures
- 1ELQ · Crystal structure of the cystine C-S lyase C-des · 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 Q9ZHG9
- Elsewhere: RCSB PDB 1ELQ · PDBe 1ELQ · UniProt Q9ZHG9
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