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Magnesium activated inorganic pyrophosphatase from thermococcus thioreducens bound to hydrolyzed product at 0.99 ångström resolution

Analyse Magnesium activated inorganic pyrophosphatase from thermococcus thioreducens… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3Q46
Type: protein
Length: 178 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tt-ippase
Ligands: MG, PO4, CL
Pockets: 1 · best druggability 0.46

Structure

x-ray diffraction · 1 distinct chain · 22% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tt-ippase	protein	178	22% helix, 34% strand	—

Ligands and binding sites

MG · Magnesium ion · metal · 4 copies · chains A
PO4 · Phosphate ion · ion · chains A
CL · Chloride ion · ion · chains A
EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	82	0.46	0.82	23	PO4, MG, CL

Compared structures

3Q46 · Magnesium activated Inorganic pyrophosphatase from Thermococcus thioreducens bound to… · 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
Elsewhere: RCSB PDB 3Q46 · PDBe 3Q46

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