Research workbench
Crystal structure of glutathione S-transferase (NP_416804.1) from escherichia COLI K12 at 1.85 a resolution
Analyse Crystal structure of glutathione S-transferase (NP_416804.1) from escherichia… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3BBY
- Type
- protein
- Length
- 191 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uncharacterized GST-like protein yfcf
- UniProt
- P77544
- Ligands
- ETX, CA
Structure
x-ray diffraction · 1 distinct chain · 54% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized GST-like protein yfcf | protein | 191 | 54% helix, 10% strand | P77544 |
Ligands and binding sites
- ETX · 2-ethoxyethanol · ligand · 2 copies · chains A
- CA · Calcium ion · metal · 2 copies · chains A
- ACT · Acetate ion · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 3 modified (engineered).
Compared structures
- 3BBY · Crystal structure of glutathione S-transferase (NP_416804.1) from Escherichia coli K12 at… · the same entry in another collection · chain A against A, TM-score 1.00
- P77544 · AlphaFold monomer V2.0 prediction for glutathione S-transferase yfcf (P77544) · 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 P77544
- Elsewhere: RCSB PDB 3BBY · PDBe 3BBY · UniProt P77544
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