Nickel in PDB 7rei: The Crystal Structure of Nickel Bound Human Ado C18S C239S Variant

All present enzymatic activity of The Crystal Structure of Nickel Bound Human Ado C18S C239S Variant:
1.13.11.19;

The structure of The Crystal Structure of Nickel Bound Human Ado C18S C239S Variant, PDB code: 7rei was solved by Y.Wang, I.Shin, J.Li, A.Liu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.62 / 1.78
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	54.881, 95.764, 117.614, 90, 90, 90
R / Rfree (%)	18 / 20.9

The binding sites of Nickel atom in the The Crystal Structure of Nickel Bound Human Ado C18S C239S Variant (pdb code 7rei). 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 The Crystal Structure of Nickel Bound Human Ado C18S C239S Variant, PDB code: 7rei:

Nickel binding site 1 out of 1 in the The Crystal Structure of Nickel Bound Human Ado C18S C239S Variant


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 1 of The Crystal Structure of Nickel Bound Human Ado C18S C239S Variant within 5.0Å range: probe atom residue distance (Å) B Occ A:Ni301 b:19.4 occ:1.00 NE2 A:HIS112 2.1 18.3 1.0 NE2 A:HIS114 2.1 18.7 1.0 O A:HOH412 2.1 18.1 1.0 NE2 A:HIS193 2.1 18.6 1.0 O A:HOH537 2.2 21.7 1.0 O A:HOH432 2.2 20.6 1.0 CE1 A:HIS114 3.0 20.2 1.0 CE1 A:HIS112 3.0 17.4 1.0 CE1 A:HIS193 3.1 22.4 1.0 CD2 A:HIS112 3.1 15.9 1.0 CD2 A:HIS193 3.1 18.3 1.0 CD2 A:HIS114 3.2 20.8 1.0 O A:HOH406 4.0 36.8 1.0 ND1 A:HIS114 4.1 20.6 1.0 ND1 A:HIS112 4.1 18.4 1.0 ND1 A:HIS193 4.2 21.3 1.0 O3 A:GOL308 4.2 36.8 1.0 CG A:HIS112 4.2 18.4 1.0 CG A:HIS193 4.2 19.9 1.0 CG A:HIS114 4.3 18.6 1.0 O2 A:GOL308 4.3 47.9 1.0 OH A:TYR212 4.3 18.8 1.0 OD2 A:ASP206 4.3 32.7 1.0 O A:HOH502 4.7 28.7 1.0 CD1 A:ILE195 4.9 25.4 1.0 C3 A:GOL308 5.0 41.5 1.0

Y.Wang, I.Shin, J.Li, A.Liu. Crystal Structure of Human Cysteamine Dioxygenase Provides A Structural Rationale For Its Function As An Oxygen Sensor J.Biol.Chem. 2021.
ISSN: ESSN 1083-351X
DOI: 10.1016/J.JBC.2021.101176