Research workbench
Crystal structure of glutathione transferase GSTFUA2 from phanerochaete chrysosporium
Analyse Crystal structure of glutathione transferase GSTFUA2 from phanerochaete… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4LMV
- Type
- protein
- Length
- 1,512 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione transferase
- EC
- 2.5.1.18
- Pockets
- 12 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 54% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Glutathione transferase (EC 2.5.1.18) | protein | 252 | 54% helix, 9% strand | — |
Ligands and binding sites
- FLC · Citrate anion · additive · 6 copies · chains A, B, C, D, E, F
- ACT · Acetate ion · additive · 5 copies · chains A, B, C, D, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1181 | 0.76 | 0.78 | 103 | FLC |
| 2 | 467 | 0.68 | 0.79 | 42 | FLC |
| 3 | 444 | 0.67 | 0.79 | 42 | FLC |
| 4 | 442 | 0.67 | 0.79 | 42 | FLC |
| 5 | 448 | 0.67 | 0.79 | 42 | FLC |
Interfaces
6 interfaces between chains.
- C–D · 994 Ų buried · 7 hydrogen bonds · protein-protein
- A–B · 979 Ų buried · 6 hydrogen bonds · protein-protein
- E–F · 951 Ų buried · 5 hydrogen bonds · protein-protein
- B–C · 364 Ų buried · 3 hydrogen bonds · protein-protein
- A–F · 82 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 4LMV · Crystal structure of glutathione transferase GSTFuA2 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 4LMV · PDBe 4LMV
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