Research workbench
Pwwp domain of human bromodomain and phd finger-containing protein 1 in complex with trimethylated H3K36 peptide
Analyse Pwwp domain of human bromodomain and phd finger-containing protein 1 in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3MO8
- Type
- protein
- Length
- 139 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peregrin; Histone H3.2 trimethylated H3K36 peptide
- UniProt
- P55201, Q71DI3
- Pockets
- 2 · best druggability 0.40
Structure
x-ray diffraction · 2 distinct chains · 33% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peregrin | protein | 127 | 36% helix, 22% strand | P55201 |
| B | Histone H3.2 trimethylated H3K36 peptide | protein | 12 | 0% helix, 8% strand | Q71DI3 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 89 | 0.40 | 0.77 | 16 | empty |
| 2 | 58 | 0.32 | 0.76 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 689 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (methylation).
Compared structures
- 3MO8 · PWWP Domain of Human Bromodomain and PHD finger-containing protein 1 In Complex with… · the same entry in another collection · chain A against A, TM-score 1.00
- P55201 · AlphaFold monomer V2.0 prediction for peregrin (P55201) · a predicted model of the same protein · chain A against A, TM-score 0.95
- Q71DI3 · AlphaFold monomer V2.0 prediction for histone H3.2 (Q71DI3) · a predicted model of the same protein · chain B against A, TM-score 0.32
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 P55201
- Every structure of UniProt Q71DI3
- Elsewhere: RCSB PDB 3MO8 · PDBe 3MO8 · UniProt P55201 · UniProt Q71DI3
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