Research workbench
Structural characterization of an engineered allosteric protein
Analyse Structural characterization of an engineered allosteric protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3CRU
- Type
- protein
- Length
- 214 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione S-transferase class-mu 26 kda isozyme
- EC
- 2.5.1.18
- UniProt
- P08515
- Ligands
- GSH
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutathione S-transferase class-mu 26 kda isozyme (EC 2.5.1.18) | protein | 214 | 50% helix, 8% strand | P08515 |
Ligands and binding sites
- GSH · Glutathione · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 3CRU · Structural characterization of an engineered allosteric protein · the same entry in another collection · chain A against A, TM-score 1.00
- P08515 · AlphaFold monomer V2.0 prediction for glutathione S-transferase class-mu 26 kda isozyme… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P08515
- Elsewhere: RCSB PDB 3CRU · PDBe 3CRU · UniProt P08515
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.