Research workbench
Crystal structure of glutathione transferase LAMBDA1 from populus trichocarpa
Analyse Crystal structure of glutathione transferase LAMBDA1 from populus trichocarpa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4PQH
- Type
- protein
- Length
- 426 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione transferase LAMBDA1
- UniProt
- B9HM14
- Ligands
- GSH, NA
- Pockets
- 2 · best druggability 0.61
Structure
x-ray diffraction · 2 distinct chains · 48% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutathione transferase LAMBDA1 | protein | 214 | 49% helix, 10% strand | B9HM14 |
| B | Glutathione transferase LAMBDA1 | protein | 212 | 48% helix, 10% strand | B9HM14 |
Ligands and binding sites
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 | 439 | 0.61 | 0.75 | 59 | GSH |
| 2 | 193 | 0.50 | 0.76 | 26 | GSH |
Interfaces
1 interface between chains.
- A–B · 696 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent (covalent ligand).
Compared structures
- 4PQH · Crystal structure of glutathione transferase lambda1 from Populus trichocarpa · 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 B9HM14
- Elsewhere: RCSB PDB 4PQH · PDBe 4PQH · UniProt B9HM14
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