Research workbench
Crystal structure of arabidopsis RDM15 tudor domain in complex with an H3K4ME1 peptide
Analyse Crystal structure of arabidopsis RDM15 tudor domain in complex with an H3K4ME1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7DE9
- Type
- protein
- Length
- 63 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcriptional regulator; Histone H3.2
- UniProt
- Q8GUP3, P59226
Structure
x-ray diffraction · 2 distinct chains · 10% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transcriptional regulator | protein | 58 | 10% helix, 52% strand | Q8GUP3 |
| P | Histone H3.2 | protein | 5 | 0% helix, 0% strand | P59226 |
Interfaces
1 interface between chains.
- A–P · 377 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (engineered, methylation).
Compared structures
- 7DE9 · crystal structure of Arabidopsis RDM15 tudor domain in complex with an H3K4me1 peptide · the same entry in another collection · chain A against A, TM-score 1.00
- P59226 · AlphaFold monomer V2.0 prediction for histone H3.2 (P59226) · a predicted model of the same protein · chain P against A, TM-score 0.83
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 Q8GUP3
- Every structure of UniProt P59226
- Elsewhere: RCSB PDB 7DE9 · PDBe 7DE9 · UniProt Q8GUP3 · UniProt P59226
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