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Tandem tudor and phd domains of UHRF2

Analyse Tandem tudor and phd domains of UHRF2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4TVR
Type: protein
Length: 222 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: E3 ubiquitin-protein ligase UHRF2
EC: 6.3.2.-
UniProt: Q96PU4
Ligands: ZN, UNX

Structure

x-ray diffraction · 1 distinct chain · 4% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	E3 ubiquitin-protein ligase UHRF2 (EC 6.3.2.-)	protein	222	4% helix, 33% strand	Q96PU4

Ligands and binding sites

ZN · Zinc ion · metal · 3 copies · chains A
UNX · Unknown atom or ion · ion · 7 copies · chains A

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

Compared structures

4TVR · Tandem Tudor and PHD domains of UHRF2 · the same entry in another collection · chain A against A, TM-score 1.00
Q96PU4 · AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase UHRF2 (Q96PU4) · a predicted model of the same protein · chain A against A, TM-score 0.80

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 Q96PU4
Elsewhere: RCSB PDB 4TVR · PDBe 4TVR · UniProt Q96PU4

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