Research workbench
Crystal structure of the pps phd finger in complex with H3K4ME3
Analyse Crystal structure of the pps phd finger 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
- 5WLE
- Type
- protein
- Length
- 66 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein partner of snf, isoform a; H3K4ME3 peptide
- EC
- 3.6.-.-
- UniProt
- Q9VG78
- Ligands
- ZN
Structure
x-ray diffraction · 2 distinct chains · 26% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein partner of snf, isoform a (EC 3.6.-.-) | protein | 59 | 29% helix, 14% strand | Q9VG78 |
| C | H3K4ME3 peptide | protein | 7 | 0% helix, 29% strand | — |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–C · 584 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (methylation).
Compared structures
- 5WLE · Crystal structure of the PPS PHD finger 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 Q9VG78
- Elsewhere: RCSB PDB 5WLE · PDBe 5WLE · UniProt Q9VG78
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