Research workbench
Crystal structure of tandem tudor domain of human UHRF1
Analyse Crystal structure of tandem tudor domain of human UHRF1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5YYA
- Type
- protein
- Length
- 160 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- E3 ubiquitin-protein ligase UHRF1
- EC
- 2.3.2.27
- UniProt
- Q96T88
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.30
Structure
x-ray diffraction · 1 distinct chain · 8% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | E3 ubiquitin-protein ligase UHRF1 (EC 2.3.2.27) | protein | 160 | 8% helix, 42% strand | Q96T88 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 67 | 0.30 | 0.73 | 15 | EDO |
Compared structures
- 5YYA · Crystal structure of Tandem Tudor Domain of human UHRF1 · 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 5YYA · PDBe 5YYA · UniProt Q96T88
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