Research workbench
The first tudor domain of PHF20L1
Analyse The first tudor domain of PHF20L1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6L0X
- Type
- protein
- Length
- 136 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phd finger protein 20-like protein 1
- UniProt
- A8MW92
- Pockets
- 1 · best druggability 0.58
Structure
x-ray diffraction · 2 distinct chains · 4% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phd finger protein 20-like protein 1 | protein | 67 | 4% helix, 40% strand | A8MW92 |
| B | Phd finger protein 20-like protein 1 | protein | 69 | 4% helix, 39% strand | A8MW92 |
Ligands and binding sites
- CIT · Citric acid · additive · 4 copies · chains A, B
- GOL · Glycerol · additive · 2 copies · chains B
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 | 279 | 0.58 | 0.77 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 272 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
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 A8MW92
- Elsewhere: RCSB PDB 6L0X · PDBe 6L0X · UniProt A8MW92
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