C-terminal kh domain of hnrnp K (KH3). Determined by solution NMR. Released 12 Jan 2000.
Explore 1KHM in 3D Show helices and sheets RCSB PDB PDBe
1KHM contains 5 α-helices and 3 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 | 7-10 | 4 | |
| β-strand | 14-21 | 8 | 1 |
| α-helix | 22-29 | 8 | |
| α-helix | 34-43 | 10 | |
| β-strand | 46-49 | 4 | 1 |
| α-helix | 50-53 | 4 | |
| β-strand | 58-65 | 8 | 1 |
| α-helix | 67-81 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein (hnrnp K) | A | protein | 89 | Homo sapiens | P61978 (AlphaFold model) |
>1KHM_1 PROTEIN (HNRNP K) (chains A) GSPNSYGDLGGPIITTQVTIPKDLARSIIGKGGQRIKQIRHESGASIKIDEPLEGSEDRI ITITGTQDQIQNAQYLLQNSVKQYSGKFF
High precision solution structure of the C-terminal KH domain of heterogeneous nuclear ribonucleoprotein K, a c-myc transcription factor. Baber, J.L., Libutti, D., Levens, D. et al. J Mol Biol (1999) 289:949-962. DOI 10.1006/jmbi.1999.2818 · PubMed
Other PDB entries of the same protein (UniProt P61978 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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