Zinc in PDB 5lxq: Structure of Prl-1 in Complex with the Bateman Domain of CNNM2

All present enzymatic activity of Structure of Prl-1 in Complex with the Bateman Domain of CNNM2:
3.1.3.48;

The structure of Structure of Prl-1 in Complex with the Bateman Domain of CNNM2, PDB code: 5lxq was solved by P.Gimenez-Mascarell, I.Oyenarte, S.Hardy, T.Breiderhoff, M.Stuiver, E.Kostantin, T.Diercks, A.L.Pey, J.Ereno-Orbea, M.L.Martinez-Chantar, R.Khalaf-Nazzal, F.Claverie-Martin, D.Muller, M.Tremblay, L.A.Martinez-Cruz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.88 / 3.34
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	166.930, 125.560, 61.040, 90.00, 111.43, 90.00
R / Rfree (%)	20.3 / 23.1

The binding sites of Zinc atom in the Structure of Prl-1 in Complex with the Bateman Domain of CNNM2 (pdb code 5lxq). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Structure of Prl-1 in Complex with the Bateman Domain of CNNM2, PDB code: 5lxq:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Structure of Prl-1 in Complex with the Bateman Domain of CNNM2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Prl-1 in Complex with the Bateman Domain of CNNM2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn602 b:79.1 occ:0.83 O2G A:ATP601 2.0 95.8 0.9 O1A A:ATP601 2.6 31.0 0.9 PG A:ATP601 3.0 96.8 0.9 O1B A:ATP601 3.0 55.3 0.9 O3G A:ATP601 3.1 67.4 0.9 O3G H:ATP601 3.1 0.9 0.9 O3B A:ATP601 3.6 89.5 0.9 PB A:ATP601 3.7 72.5 0.9 PA A:ATP601 3.8 29.2 0.9 O3A A:ATP601 3.9 45.7 0.9 PG H:ATP601 4.2 0.5 0.9 O2G H:ATP601 4.3 67.4 0.9 O1G A:ATP601 4.4 94.6 0.9 O2A A:ATP601 4.6 29.1 0.9 O1G H:ATP601 4.7 57.0 0.9 CG A:GLU570 4.8 76.2 1.0 NH2 H:ARG480 4.8 92.0 1.0

Zinc binding site 2 out of 2 in the Structure of Prl-1 in Complex with the Bateman Domain of CNNM2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of Prl-1 in Complex with the Bateman Domain of CNNM2 within 5.0Å range: probe atom residue distance (Å) B Occ H:Zn602 b:84.4 occ:0.83 O2G H:ATP601 2.0 67.4 0.9 O2A H:ATP601 2.6 39.6 0.9 O1G H:ATP601 2.7 57.0 0.9 PG H:ATP601 2.8 0.5 0.9 O2B H:ATP601 3.1 53.2 0.9 O1G A:ATP601 3.3 94.6 0.9 O3B H:ATP601 3.6 74.8 0.9 PB H:ATP601 3.8 68.5 0.9 PA H:ATP601 3.8 29.1 0.9 O3A H:ATP601 4.0 53.6 0.9 O3G H:ATP601 4.1 0.9 0.9 PG A:ATP601 4.3 96.8 0.9 O2G A:ATP601 4.3 95.8 0.9 O1A H:ATP601 4.5 29.0 0.9 O3G A:ATP601 4.6 67.4 0.9 CG H:GLU570 4.6 0.4 1.0 NH2 A:ARG480 4.9 92.2 1.0 CB H:GLU570 5.0 44.9 1.0

P.Gimenez-Mascarell, I.Oyenarte, S.Hardy, T.Breiderhoff, M.Stuiver, E.Kostantin, T.Diercks, A.L.Pey, J.Ereno-Orbea, M.L.Martinez-Chantar, R.Khalaf-Nazzal, F.Claverie-Martin, D.Muller, M.L.Tremblay, L.A.Martinez-Cruz. Structural Basis of the Oncogenic Interaction of Phosphatase Prl-1 with the Magnesium Transporter CNNM2. J. Biol. Chem. V. 292 786 2017.
ISSN: ESSN 1083-351X
PubMed: 27899452
DOI: 10.1074/JBC.M116.759944