solution structure of human MEKK3 PB1 domain. Determined by solution NMR. Released 22 May 2007.
Explore 2PPH in 3D Show helices and sheets RCSB PDB PDBe
2PPH contains 3 α-helices and 5 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 |
|---|---|---|---|
| β-strand | 4-10 | 7 | 1 |
| β-strand | 13-19 | 7 | 1 |
| α-helix | 20 | 1 | |
| α-helix | 25-36 | 12 | |
| β-strand | 40-45 | 6 | 1 |
| β-strand | 50-52 | 3 | 1 |
| α-helix | 56-68 | 13 | |
| β-strand | 75-81 | 7 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Mitogen-activated protein kinase kinase kinase 3 | A | protein | 94 | Homo sapiens | Q99759 (AlphaFold model) |
>2PPH_1 Mitogen-activated protein kinase kinase kinase 3 (chains A) MQSDVRIKFEHNGERRIIAFSRPVKYEDVEHKVTTVFGQPLDLHYMNNELSILLKNQDDL DKAIDILDRSSSMKSLRILLLSQDRNLEHHHHHH
Insight into the Binding Properties of MEKK3 PB1 to MEK5 PB1 from Its Solution Structure. Hu, Q., Shen, W., Huang, H. et al. Biochemistry (2007) 46:13478-13489. DOI 10.1021/bi701341n · PubMed
Other PDB entries of the same protein (UniProt Q99759 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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