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Solution structure of the nudix enzyme diadenosine tetraphosphate hydrolase from lupinus angustifolius complexed with ATP

Analyse Solution structure of the nudix enzyme diadenosine tetraphosphate hydrolase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1JKN
Type: protein
Length: 165 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Diadenosine 5',5'''-P1,P4-tetraphosphate hydrolase
EC: 3.6.1.17
UniProt: O04841
Ligands: ATP
Pockets: 1 · best druggability 0.63

Structure

solution nmr · 1 distinct chain · 26% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Diadenosine 5',5'''-P1,P4-tetraphosphate hydrolase (EC 3.6.1.17)	protein	165	26% helix, 28% strand	O04841

Ligands and binding sites

ATP · Adenosine-5'-triphosphate · ligand · 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	312	0.63	0.80	41	ATP

Compared structures

1JKN · Solution Structure of the Nudix Enzyme Diadenosine Tetraphosphate Hydrolase from Lupinus… · 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 O04841
Elsewhere: RCSB PDB 1JKN · PDBe 1JKN · UniProt O04841

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