Research workbench
TYR115, GLN165 and TRP209 contribute to the 1,2-epoxy-3-(P- NITROPHENOXY)PROPANE conjugating activities of glutathione S-transferase CGSTM1-1
Analyse TYR115, GLN165 and TRP209 contribute to the 1,2-epoxy-3-(P… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1C72
- Type
- protein
- Length
- 868 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P20136
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | — | protein | 217 | — | P20136 |
Compared structures
- 1C72 · TYR115, GLN165 and TRP209 contribute to the 1,2-epoxy-3-(P-NITROPHENOXY)PROPANE… · the same entry in another collection · chain A against A, TM-score 1.00
- P20136 · AlphaFold monomer V2.0 prediction for glutathione S-transferase 2 (P20136) · a predicted model of the same protein · 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 P20136
- Elsewhere: RCSB PDB 1C72 · PDBe 1C72 · UniProt P20136
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