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Structure of the glycosylase domain of MBD4

Analyse Structure of the glycosylase domain of MBD4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4E9E
Type: protein
Length: 140 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Methyl-cpg-binding domain protein 4
EC: 3.2.2.-
UniProt: O95243
Pockets: 1 · best druggability 0.36

Structure

x-ray diffraction · 1 distinct chain · 64% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Methyl-cpg-binding domain protein 4 (EC 3.2.2.-)	protein	140	64% helix, 0% strand	O95243

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	70	0.36	0.77	16	empty

Compared structures

4E9E · Structure of the glycosylase domain of MBD4 · the same entry in another collection · chain A against A, TM-score 1.00
O95243 · AlphaFold monomer V2.0 prediction for methyl-cpg-binding domain protein 4 (O95243) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 O95243
Elsewhere: RCSB PDB 4E9E · PDBe 4E9E · UniProt O95243

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