Nickel in PDB 4a2c: Crystal Structure of Galactitol-1-Phosphate Dehydrogenase From Escherichia Coli

All present enzymatic activity of Crystal Structure of Galactitol-1-Phosphate Dehydrogenase From Escherichia Coli:
1.1.1.251;

The structure of Crystal Structure of Galactitol-1-Phosphate Dehydrogenase From Escherichia Coli, PDB code: 4a2c was solved by Y.Alvarez, M.Esteban-Torres, I.Acebron, B.De Las Rivas, R.Munoz, J.M.Mancheno, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.952 / 1.87
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	43.720, 77.140, 107.510, 90.00, 95.36, 90.00
R / Rfree (%)	21.27 / 27.29

The structure of Crystal Structure of Galactitol-1-Phosphate Dehydrogenase From Escherichia Coli also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Nickel atom in the Crystal Structure of Galactitol-1-Phosphate Dehydrogenase From Escherichia Coli (pdb code 4a2c). This binding sites where shown within 5.0 Angstroms radius around Nickel atom.
In total 3 binding sites of Nickel where determined in the Crystal Structure of Galactitol-1-Phosphate Dehydrogenase From Escherichia Coli, PDB code: 4a2c:
Jump to Nickel binding site number: 1; 2; 3;

Nickel binding site 1 out of 3 in the Crystal Structure of Galactitol-1-Phosphate Dehydrogenase From Escherichia Coli


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 Galactitol-1-Phosphate Dehydrogenase From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ A:Ni1347 b:41.6 occ:1.00 NE2 A:HIS59 2.3 25.0 1.0 SG A:CYS38 2.6 34.0 1.0 OE2 A:GLU60 3.1 27.5 1.0 O A:HOH2051 3.2 38.3 1.0 CE1 A:HIS59 3.2 29.3 1.0 O A:HOH2147 3.3 35.8 1.0 CD2 A:HIS59 3.3 24.7 1.0 CB A:CYS38 3.4 27.0 1.0 OE1 A:GLU144 3.6 24.7 1.0 OE2 A:GLU144 3.8 34.7 1.0 CD A:GLU60 4.1 26.9 1.0 CD A:GLU144 4.1 30.2 1.0 CG A:GLU60 4.2 23.6 1.0 OG A:SER40 4.3 36.4 1.0 ND1 A:HIS59 4.3 25.5 1.0 CG A:HIS59 4.4 23.4 1.0 O A:HOH2066 4.8 25.8 1.0 CA A:CYS38 4.8 31.5 1.0 O A:HOH2048 4.9 27.8 1.0

Nickel binding site 2 out of 3 in the Crystal Structure of Galactitol-1-Phosphate Dehydrogenase From Escherichia Coli


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 Galactitol-1-Phosphate Dehydrogenase From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ A:Ni1348 b:25.4 occ:1.00 O A:HOH2238 2.3 18.9 1.0 ND1 A:HIS267 2.3 37.9 1.0 ND1 B:HIS267 2.4 29.9 1.0 CG A:HIS267 3.2 33.4 1.0 CE1 B:HIS267 3.2 33.1 1.0 CE1 A:HIS267 3.3 35.3 1.0 CG B:HIS267 3.3 29.6 1.0 CB A:HIS267 3.4 24.5 1.0 CB B:HIS267 3.6 29.5 1.0 NE2 B:HIS267 4.3 34.4 1.0 CD2 A:HIS267 4.3 38.4 1.0 NE2 A:HIS267 4.3 36.2 1.0 CD2 B:HIS267 4.3 32.5 1.0 CA A:HIS267 4.5 23.7 1.0 CA B:HIS267 4.6 27.6 1.0

Nickel binding site 3 out of 3 in the Crystal Structure of Galactitol-1-Phosphate Dehydrogenase From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 3 of Crystal Structure of Galactitol-1-Phosphate Dehydrogenase From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ B:Ni1347 b:34.1 occ:1.00 NE2 B:HIS59 2.3 21.7 1.0 O B:HOH2165 2.4 40.9 1.0 SG B:CYS38 2.4 27.1 1.0 OE2 B:GLU60 2.6 24.9 1.0 CD2 B:HIS59 3.1 21.0 1.0 CB B:CYS38 3.1 32.1 1.0 CE1 B:HIS59 3.4 17.8 1.0 OE1 B:GLU144 3.5 16.7 1.0 CD B:GLU60 3.6 18.0 1.0 CG B:GLU60 3.9 17.8 1.0 OE2 B:GLU144 4.2 26.0 1.0 CD B:GLU144 4.2 22.8 1.0 CG B:HIS59 4.3 16.5 1.0 ND1 B:HIS59 4.4 18.0 1.0 CA B:CYS38 4.4 31.5 1.0 OG B:SER40 4.4 25.4 1.0 O B:HOH2078 4.7 28.4 1.0 OE1 B:GLU60 4.8 18.6 1.0 O B:HOH2057 4.8 45.3 1.0

M.Esteban-Torres, Y.Alvarez, I.Acebron, B.De Las Rivas, R.Munoz, G.-W.Kohring, A.M.Roa, M.Sobrino, J.M.Mancheno. The Crystal Structure of Galactitol-1-Phosphate 5-Dehydrogenase From Escherichia Coli K12 Provides Insights Into Its Anomalous Behavior on Imac Processes Febs Lett. V. 586 3127 2012.
ISSN: ISSN
PubMed: 22979983
DOI: 10.1016/J.FEBSLET.2012.07.073