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Crystal structure of glutathione transferase GSTFUA3 from phanerochaete chrysosporium
Analyse Crystal structure of glutathione transferase GSTFUA3 from phanerochaete… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4LMW
- Type
- protein
- Length
- 250 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione transferase
- EC
- 2.5.1.18
- Pockets
- 2 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 56% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutathione transferase (EC 2.5.1.18) | protein | 250 | 56% helix, 9% strand | — |
Ligands and binding sites
- FMT · Formic acid · additive · 14 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 387 | 0.68 | 0.80 | 43 | FMT |
| 2 | 67 | 0.32 | 0.75 | 14 | empty |
Compared structures
- 4LMW · Crystal structure of glutathione transferase GSTFuA3 from Phanerochaete chrysosporium · 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
- Elsewhere: RCSB PDB 4LMW · PDBe 4LMW
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