MolNFT v1 · #87117 · protein

Legionella pneumophila NTPDASE1 crystal form I, open, ampnp complex

4BR7 · Ectonucleoside triphosphate diphosphohydrolase I: “Legionella pneumophila NTPDASE1 crystal form I, open, ampnp complex”. X-ray diffraction, 3 ligands (AU1, MG, CL), 1 pocket (best druggability 0.68). MolNFT v1 #87117 on GenesisL1…

PDB: 4BR7
Type: protein
Length: 356 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ectonucleoside triphosphate diphosphohydrolase I
EC: 3.6.1.5
UniProt: Q5ZUA2
Ligands: AU1, MG, CL
Pockets: 1 · 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 (EC 3.6.1.5)	protein	356	40% helix, 26% strand	Q5ZUA2

Ligands and binding sites

AU1 · 5'-O-[(R)-hydroxy(phosphonoamino)phosphoryl]adenosine · ligand · chains A
MG · Magnesium ion · metal · chains A
CL · Chloride ion · ion · 2 copies · 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	437	0.68	0.80	41	AU1

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

4BR7 · Legionella pneumophila NTPDase1 crystal form I, open, AMPNP complex · 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 4BR7 · PDBe 4BR7 · UniProt Q5ZUA2

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