Research workbench
Crystal structure of J-domain of dnaj homolog dnj-2 precursor from C.ELEGANS.
Analyse Crystal structure of J-domain of dnaj homolog dnj-2 precursor from C.ELEGANS. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2QSA
- Type
- protein
- Length
- 101 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dnaj homolog dnj-2
- UniProt
- Q17433
- Ligands
- CL
Structure
x-ray diffraction · 1 distinct chain · 71% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dnaj homolog dnj-2 | protein | 101 | 71% helix, 0% strand | Q17433 |
Ligands and binding sites
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 2QSA · Crystal structure of J-domain of DnaJ homolog dnj-2 precursor from C.elegans. · the same entry in another collection · chain A against A, TM-score 1.00
- Q17433 · AlphaFold monomer V2.0 prediction for dnaj homolog dnj-2 (Q17433) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 Q17433
- Elsewhere: RCSB PDB 2QSA · PDBe 2QSA · UniProt Q17433
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