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Nickel in PDB 3vj9: Crystal Structure of the Human Squalene Synthase

Enzymatic activity of Crystal Structure of the Human Squalene Synthase

All present enzymatic activity of Crystal Structure of the Human Squalene Synthase:
2.5.1.21;

Protein crystallography data

The structure of Crystal Structure of the Human Squalene Synthase, PDB code: 3vj9 was solved by C.I.Liu, W.Y.Jeng, W.J.Chang, A.H.J.Wang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.70 / 1.52
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 51.776, 76.657, 82.501, 90.00, 90.00, 90.00
R / Rfree (%) 16 / 21.4

Nickel Binding Sites:

The binding sites of Nickel atom in the Crystal Structure of the Human Squalene Synthase (pdb code 3vj9). This binding sites where shown within 5.0 Angstroms radius around Nickel atom.
In total only one binding site of Nickel was determined in the Crystal Structure of the Human Squalene Synthase, PDB code: 3vj9:

Nickel binding site 1 out of 1 in 3vj9

Go back to Nickel Binding Sites List in 3vj9
Nickel binding site 1 out of 1 in the Crystal Structure of the Human Squalene Synthase


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 1 of Crystal Structure of the Human Squalene Synthase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ni402

b:26.2
occ:1.00
OE1 A:GLU343 2.0 19.2 1.0
O A:HOH737 2.0 25.6 1.0
NE2 A:HIS347 2.1 18.4 1.0
O A:HOH487 2.1 24.2 1.0
O A:HOH734 2.2 21.3 1.0
CD A:GLU343 2.9 19.0 1.0
CE1 A:HIS347 3.0 20.7 1.0
CD2 A:HIS347 3.1 19.8 1.0
OE2 A:GLU343 3.2 21.2 1.0
O A:HOH878 4.0 37.0 1.0
ND1 A:HIS347 4.2 20.0 1.0
O A:HOH523 4.2 38.0 1.0
CG A:HIS347 4.2 19.0 1.0
CG A:GLU343 4.3 17.4 1.0
CD1 A:TYR346 4.6 20.3 1.0
O A:HOH463 4.8 30.9 1.0
CE1 A:TYR346 4.9 22.7 1.0
O A:HOH509 5.0 24.5 1.0

Reference:

C.I.Liu, W.Y.Jeng, W.J.Chang, T.P.Ko, A.H.J.Wang. Binding Modes of Zaragozic Acid A to Human Squalene Synthase and Staphylococcal Dehydrosqualene Synthase J.Biol.Chem. V. 287 18750 2012.
ISSN: ISSN 0021-9258
PubMed: 22474324
DOI: 10.1074/JBC.M112.351254
Page generated: Fri Sep 25 08:36:32 2020
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