MolNFT v1 · #90898 · protein
Crystal structure of glutathione S-transferase like protein LELG_03239 (target efi-501752) from lodderomyces elongisporus
4EXJ · Uncharacterized protein: “Crystal structure of glutathione S-transferase like protein LELG_03239 (target efi-501752) from lodderomyces…”. X-ray diffraction, 2 ligands (CL, SO4), 5 pockets (best druggability 0.66). MolNFT v1 #90898…
- PDB
- 4EXJ
- Type
- protein
- Length
- 443 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uncharacterized protein
- UniProt
- A5E0V2
- Ligands
- CL, SO4
- Pockets
- 5 · best druggability 0.66
Structure
x-ray diffraction · 2 distinct chains · 53% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized protein | protein | 221 | 53% helix, 8% strand | A5E0V2 |
| B | Uncharacterized protein | protein | 222 | 53% helix, 9% strand | A5E0V2 |
Ligands and binding sites
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 | 451 | 0.66 | 0.79 | 43 | CL, SO4 |
| 2 | 296 | 0.60 | 0.78 | 32 | SO4 |
| 3 | 188 | 0.59 | 0.82 | 29 | empty |
| 4 | 123 | 0.45 | 0.78 | 30 | empty |
| 5 | 126 | 0.45 | 0.77 | 30 | empty |
Interfaces
1 interface between chains.
- A–B · 1714 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
- 4EXJ · Crystal structure of glutathione s-transferase like protein lelg_03239 (target… · 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 A5E0V2
- Elsewhere: RCSB PDB 4EXJ · PDBe 4EXJ · UniProt A5E0V2
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