Nickel in PDB 6tto: N-Terminally Truncated Hyoscyamine 6-Hydroxylase (TH6H) in Complex with 2-Oxoglutarate

The structure of N-Terminally Truncated Hyoscyamine 6-Hydroxylase (TH6H) in Complex with 2-Oxoglutarate, PDB code: 6tto was solved by A.Kluza, B.Mrugala, P.J.Porebski, K.Kurpiewska, E.Niedzialkowska, M.S.Weiss, T.Borowski, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.70 / 1.31
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	39.896, 79.808, 104.437, 90.00, 90.00, 90.00
R / Rfree (%)	13.7 / 16.4

The structure of N-Terminally Truncated Hyoscyamine 6-Hydroxylase (TH6H) in Complex with 2-Oxoglutarate also contains other interesting chemical elements:

Strontium	(Sr)	2 atoms
Sodium	(Na)	1 atom

The binding sites of Nickel atom in the N-Terminally Truncated Hyoscyamine 6-Hydroxylase (TH6H) in Complex with 2-Oxoglutarate (pdb code 6tto). 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 N-Terminally Truncated Hyoscyamine 6-Hydroxylase (TH6H) in Complex with 2-Oxoglutarate, PDB code: 6tto:

Nickel binding site 1 out of 1 in the N-Terminally Truncated Hyoscyamine 6-Hydroxylase (TH6H) in Complex with 2-Oxoglutarate


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 1 of N-Terminally Truncated Hyoscyamine 6-Hydroxylase (TH6H) in Complex with 2-Oxoglutarate within 5.0Å range: probe atom residue distance (Å) B Occ A:Ni413 b:13.5 occ:1.00 OD1 A:ASP219 2.0 12.6 1.0 O1 A:AKG401 2.1 18.5 1.0 NE2 A:HIS217 2.1 14.3 1.0 O5 A:AKG401 2.1 17.5 1.0 NE2 A:HIS274 2.1 12.2 1.0 O A:HOH525 2.1 18.4 1.0 C2 A:AKG401 2.7 17.8 1.0 C1 A:AKG401 2.7 19.9 1.0 CG A:ASP219 3.0 12.8 1.0 CD2 A:HIS217 3.0 15.2 1.0 CE1 A:HIS217 3.0 16.4 1.0 CE1 A:HIS274 3.1 12.6 1.0 CD2 A:HIS274 3.1 11.6 1.0 HD2 A:HIS217 3.2 18.3 1.0 HE1 A:HIS217 3.2 19.6 1.0 HD2 A:HIS274 3.2 14.0 1.0 HE1 A:HIS274 3.3 15.2 1.0 OD2 A:ASP219 3.3 13.8 1.0 O2 A:AKG401 4.0 21.4 1.0 O A:HOH621 4.1 27.6 1.0 O A:HOH631 4.1 33.0 1.0 ND1 A:HIS217 4.1 16.8 1.0 ND1 A:HIS274 4.2 13.1 1.0 CG A:HIS217 4.2 14.9 1.0 C3 A:AKG401 4.2 17.8 1.0 CG A:HIS274 4.2 11.6 1.0 HD21 A:ASN256 4.3 22.1 0.6 CB A:ASP219 4.4 11.8 1.0 HA A:ASP219 4.4 13.2 1.0 H41 A:AKG401 4.5 18.6 1.0 H32 A:AKG401 4.6 21.3 1.0 H42 A:AKG401 4.6 18.6 1.0 H A:ASP219 4.6 12.7 1.0 C4 A:AKG401 4.7 15.5 1.0 N A:ASP219 4.7 10.6 1.0 CA A:ASP219 4.7 11.0 1.0 H31 A:AKG401 4.8 21.3 1.0 HG21 A:THR224 4.8 14.4 1.0 ND2 A:ASN256 4.9 18.4 0.6 HB2 A:ASP219 4.9 14.1 1.0 HD1 A:HIS217 4.9 20.1 1.0 HB3 A:ASP219 4.9 14.1 1.0 HD1 A:HIS274 4.9 15.7 1.0

A.Kluza, Z.Wojdyla, B.Mrugala, K.Kurpiewska, P.J.Porebski, E.Niedzialkowska, W.Minor, M.S.Weiss, T.Borowski. Regioselectivity of Hyoscyamine 6 Beta-Hydroxylase-Catalysed Hydroxylation As Revealed By High-Resolution Structural Information and Qm/Mm Calculations Dalton Trans 2020.
ISSN: ESSN 1477-9234
DOI: 10.1039/D0DT00302F