Research workbench

Crystal structure of the first tudor domain of human PHF20

Analyse Crystal structure of the first tudor domain of human PHF20 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3SD4
Type: protein
Length: 138 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phd finger protein 20
UniProt: Q9BVI0
Pockets: 1 · best druggability 0.42

Structure

x-ray diffraction · 1 distinct chain · 4% helix, 39% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Phd finger protein 20	protein	69	4% helix, 39% strand	Q9BVI0

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	145	0.42	0.75	27	empty

Interfaces

1 interface between chains.

A–B · 388 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

3SD4 · Crystal structure of the first Tudor domain of human PHF20 · the same entry in another collection · chain A against A, TM-score 1.00
Q9BVI0 · AlphaFold monomer V2.0 prediction for phd finger protein 20 (Q9BVI0) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 Q9BVI0
Elsewhere: RCSB PDB 3SD4 · PDBe 3SD4 · UniProt Q9BVI0

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.