Research workbench
Crystal structure of ING2 phd finger in complex with H3K4ME3 peptide
Analyse Crystal structure of ING2 phd finger in complex with H3K4ME3 peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2G6Q
- Type
- protein
- Length
- 60 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Inhibitor of growth protein 2; H3K4ME3 peptide
- UniProt
- Q9ESK4
- Ligands
- ZN
Structure
x-ray diffraction · 2 distinct chains · 12% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Inhibitor of growth protein 2 | protein | 52 | 13% helix, 21% strand | Q9ESK4 |
| B | H3K4ME3 peptide | protein | 8 | 0% helix, 50% 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–B · 554 Ų buried · 18 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (methylation).
Compared structures
- 2G6Q · Crystal structure of ING2 PHD finger in complex with H3K4Me3 peptide · the same entry in another collection · chain A against A, TM-score 1.00
- Q9ESK4 · AlphaFold monomer V2.0 prediction for inhibitor of growth protein 2 (Q9ESK4) · a predicted model of the same protein · chain A against A, TM-score 0.93
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 Q9ESK4
- Elsewhere: RCSB PDB 2G6Q · PDBe 2G6Q · UniProt Q9ESK4
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