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Stx2A1-BTB13086

Analyse Stx2A1-BTB13086 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 8CX8
Type: protein
Length: 477 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.905
Source: Escherichia coli
Molecule: rRNA N-glycosylase
EC: 3.2.2.22
UniProt: Q5WPX7
Ligands: P1U, CL, SO4
Pockets: 1 · best druggability 0.84

Structure

x-ray diffraction · resolution 1.905 · 2 distinct chains · 39% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	rRNA N-glycosylase (EC 3.2.2.22)	protein	238	39% helix, 25% strand	Q5WPX7
B	rRNA N-glycosylase (EC 3.2.2.22)	protein	239	38% helix, 24% strand	Q5WPX7

Ligands and binding sites

P1U · 5-(4-chlorophenyl)furan-2-carboxylic acid · ligand · 2 copies · chains A, B
CL · Chloride ion · ion · 9 copies · chains A, B
SO4 · Sulfate ion · ion · 8 copies · chains A, B
EDO · 1,2-ethanediol · additive · chains A

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

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	1065	0.84	0.85	111	P1U, CL, SO4

Interfaces

1 interface between chains.

A–B · 913 Å² buried · 13 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

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 Q5WPX7
Elsewhere: RCSB PDB 8CX8 · PDBe 8CX8 · UniProt Q5WPX7

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