MolNFT v1 · #18372 · protein
Glutathione transferase from proteus mirabilis
1PMT: “Glutathione transferase from proteus mirabilis”. X-ray diffraction, 1 ligand (GSH), 1 pocket (best druggability 0.46). MolNFT v1 #18372 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1PMT
- Type
- protein
- Length
- 201 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione transferase
- EC
- 2.5.1.18
- UniProt
- P15214
- Ligands
- GSH
- Pockets
- 1 · best druggability 0.46
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutathione transferase (EC 2.5.1.18) | protein | 201 | 50% helix, 10% strand | P15214 |
Ligands and binding sites
- GSH · Glutathione · ligand · 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 | 158 | 0.46 | 0.76 | 31 | GSH |
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
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 P15214
- Elsewhere: RCSB PDB 1PMT · PDBe 1PMT · UniProt P15214
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