Nickel in PDB 4zp1: Crystal Structure of Zymomonas Mobilis Pyruvate Decarboxylase Variant GLU473ALA

All present enzymatic activity of Crystal Structure of Zymomonas Mobilis Pyruvate Decarboxylase Variant GLU473ALA:
4.1.1.1;

The structure of Crystal Structure of Zymomonas Mobilis Pyruvate Decarboxylase Variant GLU473ALA, PDB code: 4zp1 was solved by C.Wechsler, P.Neumann, K.Tittmann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.55 / 2.21
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	70.290, 167.640, 110.820, 90.00, 101.66, 90.00
R / Rfree (%)	17 / 21.7

The structure of Crystal Structure of Zymomonas Mobilis Pyruvate Decarboxylase Variant GLU473ALA also contains other interesting chemical elements:

Magnesium

(Mg)

4 atoms

The binding sites of Nickel atom in the Crystal Structure of Zymomonas Mobilis Pyruvate Decarboxylase Variant GLU473ALA (pdb code 4zp1). This binding sites where shown within 5.0 Angstroms radius around Nickel atom.
In total 2 binding sites of Nickel where determined in the Crystal Structure of Zymomonas Mobilis Pyruvate Decarboxylase Variant GLU473ALA, PDB code: 4zp1:
Jump to Nickel binding site number: 1; 2;

Nickel binding site 1 out of 2 in the Crystal Structure of Zymomonas Mobilis Pyruvate Decarboxylase Variant GLU473ALA


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 Zymomonas Mobilis Pyruvate Decarboxylase Variant GLU473ALA within 5.0Å range: probe atom residue distance (Å) B Occ A:Ni602 b:60.2 occ:1.00 NE2 C:HIS106 1.9 52.0 0.5 NE2 C:HIS122 2.0 35.1 0.6 NE2 A:HIS122 2.0 37.2 0.5 NE2 A:HIS106 2.1 65.6 0.5 CE1 C:HIS106 2.7 51.3 0.5 CD2 C:HIS106 2.8 53.3 0.5 CD2 A:HIS106 2.9 66.7 0.5 CE1 A:HIS122 2.9 36.5 0.5 CE1 C:HIS122 2.9 34.5 0.6 CE1 A:HIS106 3.0 65.2 0.5 CD2 C:HIS122 3.0 36.9 0.6 CD2 A:HIS122 3.1 39.0 0.5 CD2 A:HIS106 3.5 65.8 0.5 ND1 C:HIS106 3.8 50.6 0.5 CG C:HIS106 3.9 52.9 0.5 CG A:HIS106 4.0 65.9 0.5 ND1 A:HIS106 4.0 65.5 0.5 ND1 A:HIS122 4.0 36.9 0.5 ND1 C:HIS122 4.1 33.2 0.6 CG C:HIS122 4.1 36.8 0.6 NE2 A:HIS106 4.1 64.7 0.5 CG A:HIS122 4.2 38.9 0.5 CD2 C:HIS106 4.4 50.1 0.5 CG A:HIS106 4.7 65.5 0.5 CD2 C:HIS122 5.0 38.6 0.4

Nickel binding site 2 out of 2 in the Crystal Structure of Zymomonas Mobilis Pyruvate Decarboxylase Variant GLU473ALA


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 2 of Crystal Structure of Zymomonas Mobilis Pyruvate Decarboxylase Variant GLU473ALA within 5.0Å range: probe atom residue distance (Å) B Occ B:Ni602 b:60.0 occ:1.00 NE2 D:HIS106 2.1 54.6 0.4 NE2 B:HIS106 2.1 74.3 1.0 NE2 B:HIS122 2.1 41.9 0.4 NE2 D:HIS122 2.1 37.1 0.5 CE1 D:HIS106 2.8 54.1 0.4 CE1 B:HIS122 2.8 40.5 0.4 CE1 B:HIS106 2.9 72.6 1.0 CE1 D:HIS122 2.9 31.8 0.5 CD2 B:HIS106 2.9 71.7 1.0 O B:HOH811 2.9 58.5 1.0 CD2 D:HIS106 3.0 54.7 0.4 CD2 D:HIS122 3.3 37.5 0.5 CD2 B:HIS122 3.3 41.3 0.4 ND1 D:HIS106 3.8 53.8 0.4 ND1 B:HIS106 3.8 69.7 1.0 ND1 D:HIS106 3.8 53.9 0.6 CG B:HIS106 3.9 67.3 1.0 CG D:HIS106 3.9 54.3 0.4 ND1 B:HIS122 4.1 40.3 0.4 ND1 D:HIS122 4.1 32.6 0.5 O B:HOH725 4.2 42.4 1.0 CG B:HIS122 4.3 41.4 0.4 CG D:HIS122 4.3 38.7 0.5 CE1 D:HIS106 4.4 53.0 0.6 CG D:HIS106 4.8 53.5 0.6

C.Wechsler, D.Meyer, S.Loschonsky, L.M.Funk, P.Neumann, R.Ficner, F.Brodhun, M.Muller, K.Tittmann. Tuning and Switching Enantioselectivity of Asymmetric Carboligation in An Enzyme Through Mutational Analysis of A Single Hot Spot. Chembiochem V. 16 2580 2015.
ISSN: ESSN 1439-7633
PubMed: 26488818
DOI: 10.1002/CBIC.201500529