Nickel in PDB 7qc9: Hisf-C9A-D11E-V33A_L50H_I52H Mutant in Complex with Ni(II) From T. Maritima

All present enzymatic activity of Hisf-C9A-D11E-V33A_L50H_I52H Mutant in Complex with Ni(II) From T. Maritima:
4.3.2.10;

The structure of Hisf-C9A-D11E-V33A_L50H_I52H Mutant in Complex with Ni(II) From T. Maritima, PDB code: 7qc9 was solved by M.Beaumet, A.Dose, A.Braeuer, J.Mahy, W.Ghattas, M.Groll, C.Hess, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.80
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	97.04, 97.04, 154.85, 90, 90, 120
R / Rfree (%)	15.3 / 18.9

The binding sites of Nickel atom in the Hisf-C9A-D11E-V33A_L50H_I52H Mutant in Complex with Ni(II) From T. Maritima (pdb code 7qc9). 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 Hisf-C9A-D11E-V33A_L50H_I52H Mutant in Complex with Ni(II) From T. Maritima, PDB code: 7qc9:

Nickel binding site 1 out of 1 in the Hisf-C9A-D11E-V33A_L50H_I52H Mutant in Complex with Ni(II) From T. Maritima


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 1 of Hisf-C9A-D11E-V33A_L50H_I52H Mutant in Complex with Ni(II) From T. Maritima within 5.0Å range: probe atom residue distance (Å) B Occ A:Ni301 b:57.3 occ:1.00 O A:HOH531 2.1 48.9 1.0 O A:HOH532 2.1 56.4 1.0 O A:HOH527 2.1 63.1 1.0 NE2 A:HIS50 2.2 37.3 1.0 NE2 A:HIS52 2.5 56.7 1.0 OG A:SER144 2.8 43.1 1.0 CE1 A:HIS50 3.0 39.2 1.0 CD2 A:HIS50 3.3 40.8 1.0 CE1 A:HIS52 3.3 64.4 1.0 CD2 A:HIS52 3.5 65.4 1.0 CB A:SER144 3.9 38.2 1.0 O A:HOH521 4.0 51.6 1.0 O3 A:SO4302 4.1 45.3 1.0 ND1 A:HIS50 4.1 36.7 1.0 CG A:HIS50 4.3 36.4 1.0 ND1 A:HIS52 4.5 65.5 1.0 O A:HOH520 4.5 44.7 1.0 CA A:SER144 4.6 31.2 1.0 CG A:HIS52 4.6 58.1 1.0 O A:HOH487 4.8 30.3 1.0

M.Beaumet, A.Dose, A.Brauer, J.P.Mahy, W.Ghattas, M.Groll, C.R.Hess. An Artificial Metalloprotein with Metal-Adaptive Coordination Sites and Ni-Dependent Quercetinase Activity. J.Inorg.Biochem. V. 235 11914 2022.
ISSN: ISSN 0162-0134
PubMed: 35841720
DOI: 10.1016/J.JINORGBIO.2022.111914