3QO2: M-phase phosphoprotein 8
Structural insights for MPP8 chromodomain interaction with histone H3 lysine 9. Determined by X-ray diffraction at 2.49 Å resolution. Released 6 Apr 2011.
- Method
- X-ray diffraction
- Resolution
- 2.49 Å
- Organisms
- Homo sapiens, synthetic construct
- Chains
- 8
- Atoms
- 2,460
- Mol. weight
- 37.07 kDa
- Released
- 6 Apr 2011
Explore 3QO2 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
3QO2 contains 17 α-helices and 25 β-strands across 8 chains. 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.
Chain A: 3 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 58-60 | 3 | 1 |
| β-strand | 61-70 | 10 | 2 |
| β-strand | 73-80 | 8 | 2 |
| α-helix | 85-87 | 3 | |
| β-strand | 89-92 | 4 | 2 |
| α-helix | 93-95 | 3 | |
| α-helix | 100-111 | 12 | |
Chain B: 2 helices, 5 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 58-60 | 3 | 4 |
| β-strand | 61-70 | 10 | 5 |
| β-strand | 73-80 | 8 | 5 |
| β-strand | 89-92 | 4 | 5 |
| α-helix | 93-96 | 4 | |
| β-strand | 98 | 1 | 4 |
| α-helix | 100-112 | 13 | |
Chains C and D: 4 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 58-60 | 3 | 6 |
| β-strand | 61-70 | 10 | 3 |
| β-strand | 73-80 | 8 | 3 |
| α-helix | 85-87 | 3 | |
| β-strand | 89-92 | 4 | 3 |
| α-helix | 93-95 | 3 | |
| α-helix | 97-99 | 3 | |
| α-helix | 100-113 | 14 | |
Chains P and Q: 1 helix, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 6-8 | 3 | 1 |
| α-helix | 9-10 | 2 | |
| β-strand | 13-14 | 2 | 3 |
Chain R: 0 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 6-8 | 3 | 6 |
| β-strand | 13-14 | 2 | 5 |
Chain S: 2 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 4-5 | 2 | |
| β-strand | 6-8 | 3 | 7 |
| α-helix | 9-10 | 2 | |
| β-strand | 13-14 | 2 | 2 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| M-phase phosphoprotein 8 | A, B, C, D | protein | 64 | Homo sapiens | Q99549 (AlphaFold model) |
| Histone H3 peptide | P, Q, R, S | protein | 15 | synthetic construct | P68431 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D), FASTA
>3QO2_1 M-phase phosphoprotein 8 (chains A, B, C, D)
HMGEDVFEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLEDCKEVLLEFRKKIAE
NKAK
Sequence of entity 2 (P, Q, R, S), FASTA
>3QO2_2 Histone H3 peptide (chains P, Q, R, S)
ARTKQTARKSTGGKA
Primary citation
Structural insights for MPP8 chromodomain interaction with histone H3 lysine 9: potential effect of phosphorylation on methyl-lysine binding. Chang, Y., Horton, J.R., Bedford, M.T. et al. J Mol Biol (2011) 408:807-814. DOI 10.1016/j.jmb.2011.03.018 · PubMed
Other PDB entries of the same protein (UniProt Q99549 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 6V2S 1.6 Å, Crystal Structure of chromodomain of MPP8 in complex with inhibitor UNC3866
- 9H77 2.01 Å, MPP8 chromodomain in complex with nanobody 3A02
- 7M5U 2.02 Å, Crystal structure of human MPP8 chromodomain in complex with peptidomimetic ligand UNC5246
- 3LWE 2.05 Å, The crystal structure of MPP8
- 3R93 2.06 Å, Crystal structure of the chromo domain of M-phase phosphoprotein 8 bound to H3K9Me3…
- 3SVM 2.31 Å, Human MPP8 - human DNMT3AK47me2 peptide
- 8QFB 3.04 Å, Crystal structure of human MPP8 C-terminal region (residues 565-860)
Browse structure collections
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