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1.7 ångström crystal structure of inorganic pyrophosphatase from burkholderia pseudomallei bound with phosphate

Analyse 1.7 ångström crystal structure of inorganic pyrophosphatase from burkholderia… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3GVF
Type: protein
Length: 174 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Inorganic pyrophosphatase
EC: 3.6.1.1
UniProt: Q3JUV5
Ligands: K, NA, PO4
Pockets: 1 · best druggability 0.53

Structure

x-ray diffraction · 1 distinct chain · 21% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Inorganic pyrophosphatase (EC 3.6.1.1)	protein	174	21% helix, 35% strand	Q3JUV5

Ligands and binding sites

K · Potassium ion · metal · chains A
NA · Sodium ion · metal · chains A
PO4 · Phosphate ion · ion · chains A
PGE · Triethylene glycol · additive · 2 copies · chains A
PEG · Di(hydroxyethyl)ether · 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	186	0.53	0.79	33	PO4

Compared structures

3GVF · 1.7 Angstrom crystal structure of inorganic pyrophosphatase from burkholderia… · 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 Q3JUV5
Elsewhere: RCSB PDB 3GVF · PDBe 3GVF · UniProt Q3JUV5

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