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Crystal structure of pyrophosphatase from bacteroides thetaiotaomicron, ASP13ASN mutant complexed with magnesium and tartrate

Analyse Crystal structure of pyrophosphatase from bacteroides thetaiotaomicron… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3QU9
Type: protein
Length: 225 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Inorganic pyrophosphatase
EC: 3.6.1.1
UniProt: Q8A5V9
Ligands: MG, CL
Pockets: 1 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Inorganic pyrophosphatase (EC 3.6.1.1)	protein	225	50% helix, 12% strand	Q8A5V9

Ligands and binding sites

MG · Magnesium ion · metal · chains A
CL · Chloride ion · ion · chains A
GOL · Glycerol · additive · chains A
TLA · L(+)-tartaric acid · 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	77	0.71	0.96	20	TLA, CL

Compared structures

3QU9 · Crystal structure of pyrophosphatase from bacteroides thetaiotaomicron, asp13asn mutant… · the same entry in another collection · chain A against A, TM-score 1.00

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 Q8A5V9
Elsewhere: RCSB PDB 3QU9 · PDBe 3QU9 · UniProt Q8A5V9

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