Research workbench

Adenine-specific DNA methyltransferase M.BseCI

Analyse Adenine-specific DNA methyltransferase M.BseCI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7QW8
Type: protein
Length: 1,061 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.5
Source: Geobacillus stearothermophilus
Molecule: Modification methylase BseCI
EC: 2.1.1.72
UniProt: P43423
Pockets: 10 · best druggability 0.59

Structure

x-ray diffraction · resolution 2.5 · 2 distinct chains · 39% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Modification methylase BseCI (EC 2.1.1.72)	protein	525	39% helix, 24% strand	P43423
B	Modification methylase BseCI (EC 2.1.1.72)	protein	536	39% helix, 24% strand	P43423

Pockets

10 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	405	0.59	0.75	52	empty
2	67	0.59	0.90	22	empty
3	354	0.56	0.75	29	empty
4	202	0.56	0.79	41	empty
5	211	0.51	0.76	45	empty

Interfaces

1 interface between chains.

A–B · 288 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

P43423 · AlphaFold monomer V2.0 prediction for modification methylase bseci (P43423) · a predicted model of the same protein · chain A against A, TM-score 0.84

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 P43423
Elsewhere: RCSB PDB 7QW8 · PDBe 7QW8 · UniProt P43423

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