Nickel in PDB 3leo: Structure of Human Leukotriene C4 Synthase Mutant R31Q in Complex with Glutathione

All present enzymatic activity of Structure of Human Leukotriene C4 Synthase Mutant R31Q in Complex with Glutathione:
4.4.1.20;

The structure of Structure of Human Leukotriene C4 Synthase Mutant R31Q in Complex with Glutathione, PDB code: 3leo was solved by D.Niegowski, D.Martinez-Molina, A.Rinaldo-Matthis, P.Nordlund, J.Haeggstrom, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.10
Space group	F 2 3
Cell size a, b, c (Å), α, β, γ (°)	169.540, 169.540, 169.540, 90.00, 90.00, 90.00
R / Rfree (%)	17.2 / 19.6

The binding sites of Nickel atom in the Structure of Human Leukotriene C4 Synthase Mutant R31Q in Complex with Glutathione (pdb code 3leo). This binding sites where shown within 5.0 Angstroms radius around Nickel atom.
In total 2 binding sites of Nickel where determined in the Structure of Human Leukotriene C4 Synthase Mutant R31Q in Complex with Glutathione, PDB code: 3leo:
Jump to Nickel binding site number: 1; 2;

Nickel binding site 1 out of 2 in the Structure of Human Leukotriene C4 Synthase Mutant R31Q in Complex with Glutathione


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 1 of Structure of Human Leukotriene C4 Synthase Mutant R31Q in Complex with Glutathione within 5.0Å range: probe atom residue distance (Å) B Occ A:Ni210 b:0.9 occ:0.33 NE2 A:HIS1 2.0 49.8 1.0 NE2 A:HIS-1 2.4 53.8 1.0 CD2 A:HIS1 2.7 48.2 1.0 CE1 A:HIS1 3.1 49.0 1.0 CD2 A:HIS-1 3.2 53.6 1.0 CE1 A:HIS-1 3.4 53.3 1.0 CG A:HIS1 3.9 49.0 1.0 ND1 A:HIS1 4.0 49.7 1.0 CG A:HIS-1 4.4 57.7 1.0 ND1 A:HIS-1 4.5 53.5 1.0

Nickel binding site 2 out of 2 in the Structure of Human Leukotriene C4 Synthase Mutant R31Q in Complex with Glutathione


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 2 of Structure of Human Leukotriene C4 Synthase Mutant R31Q in Complex with Glutathione within 5.0Å range: probe atom residue distance (Å) B Occ A:Ni211 b:0.0 occ:0.33 NE2 A:HIS-2 2.5 0.5 1.0 NE2 A:HIS-4 2.7 42.2 1.0 CD2 A:HIS-2 3.2 0.7 1.0 CD2 A:HIS-4 3.3 49.5 1.0 CE1 A:HIS-2 3.7 0.2 1.0 CE1 A:HIS-4 3.8 50.0 1.0 CG A:HIS-2 4.5 89.5 1.0 CG A:HIS-4 4.5 58.9 1.0 ND1 A:HIS-2 4.6 0.8 1.0 ND1 A:HIS-4 4.7 55.5 1.0

A.Rinaldo-Matthis, A.Wetterholm, D.Martinez Molina, J.Holm, D.Niegowski, E.Ohlson, P.Nordlund, R.Morgenstern, J.Z.Haeggstrom. Arginine 104 Is A Key Catalytic Residue in Leukotriene C4 Synthase. J.Biol.Chem. V. 285 40771 2010.
ISSN: ISSN 0021-9258
PubMed: 20980252
DOI: 10.1074/JBC.M110.105940