Research workbench

Crystal structure of LP1NTPDASE from legionella pneumophila in complex with amppnp

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

PDB: 3AAR
Type: protein
Length: 352 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ectonucleoside triphosphate diphosphohydrolase I
UniProt: Q5ZUA2
Ligands: ANP
Pockets: 2 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ectonucleoside triphosphate diphosphohydrolase I	protein	352	40% helix, 26% strand	Q5ZUA2

Ligands and binding sites

ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	454	0.68	0.80	44	ANP
2	117	0.48	0.79	18	empty

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

3AAR · Crystal structure of Lp1NTPDase from Legionella pneumophila in complex with AMPPNP · 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 3AAR · PDBe 3AAR · UniProt Q5ZUA2

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