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Inorganic pyrophosphatase from the pathogenic bacterium helicobacter pylori-kinetic and structural properties

Analyse Inorganic pyrophosphatase from the pathogenic bacterium helicobacter… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2BQY
Type: protein
Length: 170 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Inorganic pyrophosphatase
EC: 3.6.1.1
UniProt: P56153
Ligands: POP
Pockets: 2 · best druggability 0.57

Structure

x-ray diffraction · 1 distinct chain · 19% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Inorganic pyrophosphatase (EC 3.6.1.1)	protein	170	19% helix, 35% strand	P56153

Ligands and binding sites

POP · Pyrophosphate 2- · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	227	0.57	0.79	38	POP
2	53	0.34	0.78	17	empty

Compared structures

2BQY · Inorganic Pyrophosphatase from the Pathogenic Bacterium Helicobacter pylori-Kinetic and… · the same entry in another collection · chain A against A, TM-score 1.00
P56153 · AlphaFold monomer V2.0 prediction for inorganic pyrophosphatase (P56153) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P56153
Elsewhere: RCSB PDB 2BQY · PDBe 2BQY · UniProt P56153

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