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Crystal structure of wildtype ment in the native conformation

Analyse Crystal structure of wildtype ment in the native conformation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2H4R
Type: protein
Length: 371 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Heterochromatin-associated protein ment
UniProt: O73790
Pockets: 1 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Heterochromatin-associated protein ment	protein	371	30% helix, 32% strand	O73790

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	153	0.50	0.79	27	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

2H4R · Crystal structure of wildtype MENT in the native conformation · the same entry in another collection · chain A against A, TM-score 1.00
O73790 · AlphaFold monomer V2.0 prediction for heterochromatin-associated protein ment (O73790) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 O73790
Elsewhere: RCSB PDB 2H4R · PDBe 2H4R · UniProt O73790

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