MolNFT v1 · #80895 · protein
Crystal structure of glutathione transferase (target efi-501774) from methylococcus capsulatus str. bath
3UAP · Glutathione S-transferase: “Crystal structure of glutathione transferase (target efi-501774) from methylococcus capsulatus str. bath”. X-ray diffraction, 1 pocket (best druggability 0.54). MolNFT v1 #80895 on GenesisL1: 3D…
- PDB
- 3UAP
- Type
- protein
- Length
- 203 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione S-transferase
- EC
- 2.5.1.18
- UniProt
- Q60CN1
- Pockets
- 1 · best druggability 0.54
Structure
x-ray diffraction · 1 distinct chain · 53% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutathione S-transferase (EC 2.5.1.18) | protein | 203 | 53% helix, 11% strand | Q60CN1 |
Ligands and binding sites
- GOL · Glycerol · additive · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 298 | 0.54 | 0.75 | 42 | empty |
Compared structures
- 3UAP · Crystal structure of glutathione transferase (TARGET EFI-501774) from methylococcus… · 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 Q60CN1
- Elsewhere: RCSB PDB 3UAP · PDBe 3UAP · UniProt Q60CN1
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