Research workbench
Crystal structure of PHF13 in complex with H3K4ME3
Analyse Crystal structure of PHF13 in complex with H3K4ME3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3O7A
- Type
- protein
- Length
- 58 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phd finger protein 13 variant; H3K4ME3 histone 11MER-peptide
- UniProt
- Q59FB6, Q92133
- Ligands
- ZN
Structure
x-ray diffraction · 2 distinct chains · 12% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phd finger protein 13 variant | protein | 52 | 13% helix, 15% strand | Q59FB6 |
| B | H3K4ME3 histone 11MER-peptide | protein | 6 | 0% helix, 33% strand | Q92133 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 511 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (methylation).
Compared structures
- 3O7A · Crystal structure of PHF13 in complex with H3K4me3 · the same entry in another collection · chain A against A, TM-score 1.00
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 Q59FB6
- Every structure of UniProt Q92133
- Elsewhere: RCSB PDB 3O7A · PDBe 3O7A · UniProt Q59FB6 · UniProt Q92133
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