Research workbench
Peroxiredoxin from aeropyrum pernix K1 (apprx) C50S/F80C/C207S/C213S mutant modified with 2-BROMOACETOPHENONE(PH@APPRX*)
Analyse Peroxiredoxin from aeropyrum pernix K1 (apprx) C50S/F80C/C207S/C213S mutant… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7C89
- Type
- protein
- Length
- 2,440 residues
- Chains
- 10
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9Y9L0
- Ligands
- FL0
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J | — | protein | 244 | — | Q9Y9L0 |
Ligands and binding sites
- FL0 · 2-bromanyl-1-phenyl-ethanone · ligand · 10 copies · chains A, D, B, J, C, G, E, I, F, H
- FLC · Citrate anion · additive · 10 copies · chains A, B, C, D, E, F, G, H, I, J
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7C89 · Peroxiredoxin from Aeropyrum pernix K1 (ApPrx) C50S/F80C/C207S/C213S mutant modified with… · 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 Q9Y9L0
- Elsewhere: RCSB PDB 7C89 · PDBe 7C89 · UniProt Q9Y9L0
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.