Research workbench

Crystal structure of LP1NTPDASE from legionella pneumophila in complex with the inhibitor arl 67156

Analyse Crystal structure of LP1NTPDASE from legionella pneumophila in complex with the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3AAQ
Type: protein
Length: 349 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ectonucleoside triphosphate diphosphohydrolase I
UniProt: Q5ZUA2
Ligands: ARU
Pockets: 1 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ectonucleoside triphosphate diphosphohydrolase I	protein	349	41% helix, 26% strand	Q5ZUA2

Ligands and binding sites

ARU · 5'-O-[(R)-{[(R)-[dibromo(phosphono)methyl](hydroxy)phosphoryl]oxy}(hydroxy)phosphoryl]-N,N-diethyladenosine · 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	382	0.64	0.79	43	ARU

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

3AAQ · Crystal structure of Lp1NTPDase from Legionella pneumophila in complex with the inhibitor… · 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 Q5ZUA2
Elsewhere: RCSB PDB 3AAQ · PDBe 3AAQ · UniProt Q5ZUA2

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.