Human HSP40 (hdj-1), NMR. Determined by solution NMR. Released 8 Nov 1996.
Explore 1HDJ in 3D Show helices and sheets RCSB PDB PDBe
1HDJ contains 5 α-helices and 2 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 5-8 | 4 | |
| β-strand | 12 | 1 | 1 |
| β-strand | 14 | 1 | 1 |
| α-helix | 16-28 | 13 | |
| α-helix | 40-53 | 14 | |
| α-helix | 57-65 | 9 | |
| α-helix | 68-70 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Human HSP40 | A | protein | 77 | Homo sapiens | P25685 (AlphaFold model) |
>1HDJ_1 HUMAN HSP40 (chains A) MGKDYYQTLGLARGASDEEIKRAYRRQALRYHPDKNKEPGAEEKFKEIAEAYDVLSDPRK REIFDRYGEEGLKGSGC
Nuclear magnetic resonance solution structure of the human Hsp40 (HDJ-1) J-domain. Qian, Y.Q., Patel, D., Hartl, F.U. et al. J Mol Biol (1996) 260:224-235. DOI 10.1006/jmbi.1996.0394 · PubMed
Other PDB entries of the same protein (UniProt P25685 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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