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Crystal structure of a nucleoside triphosphate diphosphohydrolase (ntpdase) from the legume trifolium repens

Analyse Crystal structure of a nucleoside triphosphate diphosphohydrolase (ntpdase)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5U7P
Type
protein
Length
405 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Apyrase
EC
3.6.1.5
UniProt
B9U139
Ligands
PO4
Pockets
3 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 26% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AApyrase (EC 3.6.1.5)protein40537% helix, 26% strandB9U139

Ligands and binding sites

  • PO4 · Phosphate ion · ion · 2 copies · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13730.560.7548PO4
2720.340.7623empty
3520.270.7415empty

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

  • 5U7P · Crystal structure of a nucleoside triphosphate diphosphohydrolase (NTPDase) from the… · the same entry in another collection · chain A against A, TM-score 1.00

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