Nickel in PDB 6ttn: N-Terminally Truncated Hyoscyamine 6-Hydroxylase (TH6H) in Complex with N-Oxalylglycine and Hyoscyamine

The structure of N-Terminally Truncated Hyoscyamine 6-Hydroxylase (TH6H) in Complex with N-Oxalylglycine and Hyoscyamine, PDB code: 6ttn 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)	43.78 / 1.12
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	39.894, 79.841, 104.701, 90.00, 90.00, 90.00
R / Rfree (%)	12.7 / 14.6

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

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

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

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


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 N-Oxalylglycine and Hyoscyamine within 5.0Å range: probe atom residue distance (Å) B Occ A:Ni508 b:10.8 occ:1.00 NE2 A:HIS274 2.1 9.9 1.0 O1 A:OGA501 2.1 13.1 1.0 OD1 A:ASP219 2.1 10.4 1.0 NE2 A:HIS217 2.1 11.0 1.0 O2' A:OGA501 2.1 11.8 1.0 O A:HOH642 2.1 13.0 1.0 C2 A:OGA501 2.8 13.0 1.0 C1 A:OGA501 2.8 14.9 1.0 CD2 A:HIS274 3.0 10.3 1.0 CE1 A:HIS217 3.1 11.8 1.0 CG A:ASP219 3.1 10.7 1.0 CE1 A:HIS274 3.1 10.8 1.0 CD2 A:HIS217 3.1 10.6 1.0 HD2 A:HIS274 3.2 12.4 1.0 HE1 A:HIS217 3.2 14.2 1.0 HD2 A:HIS217 3.3 12.7 1.0 HE1 A:HIS274 3.3 12.9 1.0 OD2 A:ASP219 3.4 11.9 1.0 H9 A:HYO506 3.5 14.2 1.0 H17 A:HYO506 3.8 15.1 1.0 O A:HOH912 4.0 18.1 1.0 N1 A:OGA501 4.0 12.7 1.0 O2 A:OGA501 4.1 19.5 1.0 ND1 A:HIS217 4.2 11.8 1.0 ND1 A:HIS274 4.2 11.1 1.0 H10 A:HYO506 4.2 13.4 1.0 CG A:HIS274 4.2 10.2 1.0 CG A:HIS217 4.2 10.7 1.0 HD21 A:ASN256 4.4 21.5 1.0 CB A:ASP219 4.5 9.9 1.0 C07 A:HYO506 4.5 11.8 1.0 HA A:ASP219 4.5 11.3 1.0 H1 A:OGA501 4.6 15.2 1.0 H4C1 A:OGA501 4.6 14.9 1.0 H A:ASP219 4.7 11.2 1.0 H4C2 A:OGA501 4.7 14.9 1.0 C12 A:HYO506 4.7 12.6 1.0 C4 A:OGA501 4.7 12.4 1.0 N A:ASP219 4.8 9.3 1.0 H15 A:HYO506 4.8 15.1 1.0 CA A:ASP219 4.8 9.4 1.0 C08 A:HYO506 4.8 11.2 1.0 HG21 A:THR224 4.8 12.5 1.0 HB2 A:ASP219 4.9 11.9 1.0 HD1 A:HIS217 5.0 14.2 1.0 H8 A:HYO506 5.0 14.2 1.0 HD1 A:HIS274 5.0 13.4 1.0 HB3 A:ASP219 5.0 11.9 1.0 ND2 A:ASN256 5.0 17.9 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