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Crystal structure of tudor domain 2 of human phd finger protein 20

Analyse Crystal structure of tudor domain 2 of human phd finger protein 20 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3QII
Type
protein
Length
52 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Phd finger protein 20
UniProt
Q9BVI0
Ligands
UNX

Structure

x-ray diffraction · 1 distinct chain · 6% helix, 54% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APhd finger protein 20protein526% helix, 54% strandQ9BVI0

Ligands and binding sites

  • UNX · Unknown atom or ion · ion · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Compared structures

  • 3QII · Crystal structure of tudor domain 2 of human PHD finger protein 20 · 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 0.90

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