Zinc in PDB 4lr2: Crystal Structure of Human ENPP4 (Apo)

All present enzymatic activity of Crystal Structure of Human ENPP4 (Apo):
3.6.1.29;

The structure of Crystal Structure of Human ENPP4 (Apo), PDB code: 4lr2 was solved by R.A.Albright, D.T.Braddock, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	22.73 / 1.50
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	181.506, 51.293, 53.065, 90.00, 102.08, 90.00
R / Rfree (%)	15.4 / 20.1

The binding sites of Zinc atom in the Crystal Structure of Human ENPP4 (Apo) (pdb code 4lr2). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Human ENPP4 (Apo), PDB code: 4lr2:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Human ENPP4 (Apo)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Human ENPP4 (Apo) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn505 b:15.0 occ:1.00 OG1 A:THR70 1.9 11.5 1.0 NE2 A:HIS238 2.0 9.3 1.0 OD2 A:ASP237 2.0 12.2 1.0 OD1 A:ASP34 2.0 16.9 1.0 CG A:ASP34 2.7 12.8 1.0 OD2 A:ASP34 2.7 26.1 1.0 CG A:ASP237 2.8 14.9 1.0 CD2 A:HIS238 2.9 12.8 1.0 CE1 A:HIS238 3.0 9.2 1.0 CB A:THR70 3.0 13.9 1.0 OD1 A:ASP237 3.0 14.2 1.0 CG2 A:THR70 3.4 15.9 1.0 CA A:THR70 3.4 12.4 1.0 OA1 A:FLC507 3.8 30.3 1.0 O A:HOH732 4.0 23.5 1.0 N A:THR70 4.0 10.6 1.0 CG A:HIS238 4.0 13.4 1.0 ND1 A:HIS238 4.0 11.4 1.0 CB A:ASP34 4.1 13.6 1.0 OD1 A:ASP189 4.2 20.4 1.0 CG A:ASP189 4.2 19.5 1.0 CB A:ASP237 4.2 12.3 1.0 CE1 A:HIS336 4.2 13.6 1.0 N A:GLY35 4.2 11.3 1.0 OD2 A:ASP189 4.4 26.9 1.0 NE2 A:HIS336 4.5 16.2 1.0 CE1 A:HIS74 4.5 18.6 1.0 CA A:ASP34 4.5 11.1 1.0 ZN A:ZN506 4.6 17.5 1.0 CAC A:FLC507 4.7 26.1 1.0 OA2 A:FLC507 4.7 21.1 1.0 C A:ASP34 4.7 12.2 1.0 C A:THR70 4.7 13.9 1.0 CB A:ASP189 4.7 14.6 1.0 C A:LYS69 4.7 10.8 1.0 CA A:GLY35 4.8 13.3 1.0 ND1 A:HIS74 4.9 15.8 1.0 ND1 A:HIS336 5.0 11.7 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Human ENPP4 (Apo)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Human ENPP4 (Apo) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn506 b:17.5 occ:1.00 NE2 A:HIS336 2.1 16.2 1.0 NE2 A:HIS193 2.1 12.2 1.0 OB2 A:FLC507 2.2 28.9 1.0 OD2 A:ASP189 2.3 26.9 1.0 OHB A:FLC507 2.5 29.9 1.0 OD1 A:ASP189 2.6 20.4 1.0 OA1 A:FLC507 2.6 30.3 1.0 CG A:ASP189 2.8 19.5 1.0 CD2 A:HIS193 3.0 13.8 1.0 CE1 A:HIS336 3.0 13.6 1.0 CD2 A:HIS336 3.1 14.8 1.0 CE1 A:HIS193 3.1 14.6 1.0 CBC A:FLC507 3.1 28.8 1.0 CB A:FLC507 3.4 27.4 1.0 CAC A:FLC507 3.5 26.1 1.0 O A:HOH732 4.0 23.5 1.0 CA A:FLC507 4.1 24.7 1.0 OG1 A:FLC507 4.2 36.0 1.0 ND1 A:HIS336 4.2 11.7 1.0 CG A:HIS193 4.2 14.8 1.0 O A:HOH855 4.2 29.6 1.0 ND1 A:HIS193 4.2 14.0 1.0 CG A:HIS336 4.2 12.2 1.0 CE1 A:HIS238 4.2 9.2 1.0 CB A:ASP189 4.3 14.6 1.0 OB1 A:FLC507 4.3 31.7 1.0 OA2 A:FLC507 4.3 21.1 1.0 OG1 A:THR70 4.4 11.5 1.0 NE2 A:HIS238 4.4 9.3 1.0 O A:HOH670 4.6 24.6 1.0 ZN A:ZN505 4.6 15.0 1.0 CG A:FLC507 4.7 25.8 1.0 CE A:MET240 4.7 12.7 1.0 OD1 A:ASP34 4.8 16.9 1.0 CGC A:FLC507 4.8 36.3 1.0 O A:ASP189 5.0 12.8 1.0

R.A.Albright, D.L.Ornstein, W.Cao, W.C.Chang, D.Robert, M.Tehan, D.Hoyer, L.Liu, P.Stabach, G.Yang, E.M.De La Cruz, D.T.Braddock. Molecular Basis of Purinergic Signal Metabolism By Ectonucleotide Pyrophosphatase/Phosphodiesterases 4 and 1 and Implications in Stroke. J.Biol.Chem. V. 289 3294 2014.
ISSN: ISSN 0021-9258
PubMed: 24338010
DOI: 10.1074/JBC.M113.505867