Research workbench
NMR structure of UHRF1 phd domains in a complex with histone H3 peptide
Analyse NMR structure of UHRF1 phd domains in a complex with histone H3 peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2LGK
- Type
- protein
- Length
- 81 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- E3 ubiquitin-protein ligase UHRF1; Histone H3 peptide
- EC
- 6.3.2.-
- UniProt
- Q96T88
- Ligands
- ZN
- Pockets
- 1 · best druggability 0.58
Structure
solution nmr · 2 distinct chains · 9% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | E3 ubiquitin-protein ligase UHRF1 (EC 6.3.2.-) | protein | 69 | 10% helix, 6% strand | Q96T88 |
| B | Histone H3 peptide | protein | 12 | 0% helix, 0% strand | — |
Ligands and binding sites
- ZN · Zinc ion · metal · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 99 | 0.58 | 0.86 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 606 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (methylation).
Compared structures
- 2LGK · NMR Structure of UHRF1 PHD domains in a complex with histone H3 peptide · the same entry in another collection · chain A against A, TM-score 1.00
- Q96T88 · AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase UHRF1 (Q96T88) · a predicted model of the same protein · chain A against A, TM-score 0.59
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 Q96T88
- Elsewhere: RCSB PDB 2LGK · PDBe 2LGK · UniProt Q96T88
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