MolNFT v2 · #155977 · protein
Peroxiredoxin from Aeropyrum pernix K1 (ApPrx) 0Cys F80A mutant
6KRQ: “Peroxiredoxin from Aeropyrum pernix K1 (ApPrx) 0Cys F80A mutant”. X-ray diffraction at 2.1. MolNFT v2 #155977 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6KRQ
- Type
- protein
- Length
- 2,440 residues
- Chains
- 10
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.1
- Source
- Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
- UniProt
- Q9Y9L0
Structure
x-ray diffraction · resolution 2.1 · 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
- CIT · Citric acid · 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
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 6KRQ · PDBe 6KRQ · UniProt Q9Y9L0
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