MolNFT v1 · #98398 · protein
Crystal structure of a glutathione transferase family member from xenorhabdus nematophila, target efi-507418, with two gsh per subunit
4L8E · Glutathione S-transferase enzyme with thioredoxin-like…: “Crystal structure of a glutathione transferase family member from xenorhabdus nematophila, target efi-507418…”. X-ray diffraction, 2 ligands (GSH, CL), 1 pocket (best…
- PDB
- 4L8E
- Type
- protein
- Length
- 203 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione S-transferase enzyme with thioredoxin-like domain
- UniProt
- D3VKV1
- Ligands
- GSH, CL
- Pockets
- 1 · best druggability 0.48
Structure
x-ray diffraction · 1 distinct chain · 58% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutathione S-transferase enzyme with thioredoxin-like domain | protein | 203 | 58% helix, 9% strand | D3VKV1 |
Ligands and binding sites
- GSH · Glutathione · ligand · 3 copies · chains A
- CL · Chloride ion · ion · chains A
- MES · 2-(N-morpholino)-ethanesulfonic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 193 | 0.48 | 0.76 | 24 | GSH |
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 4L8E · Crystal structure of a glutathione transferase family member from xenorhabdus… · 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 D3VKV1
- Elsewhere: RCSB PDB 4L8E · PDBe 4L8E · UniProt D3VKV1
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