Research workbench
Crystal structure of tandem tudor domain of human UHRF1 in complex with LIG1-K126ME3
Analyse Crystal structure of tandem tudor domain of human UHRF1 in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5YY9
- Type
- protein
- Length
- 297 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- E3 ubiquitin-protein ligase UHRF1; Ligase 1
- EC
- 2.3.2.27
- UniProt
- Q96T88
- Pockets
- 1 · best druggability 0.54
Structure
x-ray diffraction · 4 distinct chains · 4% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | E3 ubiquitin-protein ligase UHRF1 (EC 2.3.2.27) | protein | 137 | 4% helix, 52% strand | Q96T88 |
| B | E3 ubiquitin-protein ligase UHRF1 (EC 2.3.2.27) | protein | 138 | 4% helix, 46% strand | Q96T88 |
| C | Ligase 1 | protein | 12 | 0% helix, 0% strand | — |
| D | Ligase 1 | protein | 10 | 0% helix, 0% strand | — |
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 | 248 | 0.54 | 0.77 | 36 | empty |
Interfaces
4 interfaces between chains.
- A–C · 742 Ų buried · 12 hydrogen bonds · protein-protein
- B–D · 727 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 568 Ų buried · 5 hydrogen bonds · protein-protein
- A–D · 34 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (methylation).
Compared structures
- 5YY9 · Crystal structure of Tandem Tudor Domain of human UHRF1 in complex with LIG1-K126me3 · 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 Q96T88
- Elsewhere: RCSB PDB 5YY9 · PDBe 5YY9 · UniProt Q96T88
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.