Zinc in PDB 6nuu: Structure of Calcineurin Mutant in Complex with NHE1 Peptide

All present enzymatic activity of Structure of Calcineurin Mutant in Complex with NHE1 Peptide:
3.1.3.16;

The structure of Structure of Calcineurin Mutant in Complex with NHE1 Peptide, PDB code: 6nuu was solved by X.Wang, R.Page, W.Peti, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.80 / 2.30
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	79.303, 125.966, 127.352, 90.00, 90.00, 90.00
R / Rfree (%)	19.5 / 24.3

The structure of Structure of Calcineurin Mutant in Complex with NHE1 Peptide also contains other interesting chemical elements:

Iron	(Fe)	1 atom
Calcium	(Ca)	4 atoms

The binding sites of Zinc atom in the Structure of Calcineurin Mutant in Complex with NHE1 Peptide (pdb code 6nuu). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Structure of Calcineurin Mutant in Complex with NHE1 Peptide, PDB code: 6nuu:

Zinc binding site 1 out of 1 in the Structure of Calcineurin Mutant in Complex with NHE1 Peptide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Calcineurin Mutant in Complex with NHE1 Peptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn402 b:30.4 occ:1.00 NE2 A:HIS199 2.1 21.8 1.0 O1 A:PO4403 2.1 24.6 0.8 OD1 A:ASN150 2.1 23.3 1.0 O A:HOH553 2.2 21.4 1.0 ND1 A:HIS281 2.2 22.6 1.0 OD2 A:ASP118 2.3 23.0 1.0 HE1 A:HIS281 2.8 27.3 1.0 CE1 A:HIS281 2.8 22.8 1.0 HA A:HIS281 2.9 26.5 1.0 CE1 A:HIS199 2.9 20.4 1.0 HD21 A:ASN150 3.0 30.3 1.0 HE1 A:HIS199 3.1 24.5 1.0 CG A:ASN150 3.1 24.2 1.0 CD2 A:HIS199 3.2 21.4 1.0 FE A:FE401 3.2 24.7 0.7 CG A:ASP118 3.2 22.3 1.0 P A:PO4403 3.3 27.0 0.8 ND2 A:ASN150 3.4 25.3 1.0 CG A:HIS281 3.4 22.5 1.0 HD2 A:HIS199 3.4 25.7 1.0 HD2 A:HIS151 3.5 29.9 1.0 O4 A:PO4403 3.6 25.3 0.8 OD1 A:ASP118 3.6 22.7 1.0 CA A:HIS281 3.8 22.1 1.0 H A:ASN150 3.8 27.5 1.0 O2 A:PO4403 4.0 25.7 0.8 OD2 A:ASP90 4.0 19.4 1.0 CB A:HIS281 4.0 22.1 1.0 NE2 A:HIS281 4.0 23.2 1.0 O A:HIS281 4.1 23.7 1.0 ND1 A:HIS199 4.1 19.6 1.0 HB2 A:HIS281 4.1 26.6 1.0 CG A:HIS199 4.2 20.8 1.0 HD22 A:ASN150 4.2 30.3 1.0 CD2 A:HIS281 4.3 23.5 1.0 CD2 A:HIS151 4.4 24.9 1.0 C A:HIS281 4.4 22.4 1.0 HB2 A:ASP118 4.4 25.4 1.0 CB A:ASN150 4.5 24.7 1.0 CB A:ASP118 4.5 21.2 1.0 O3 A:PO4403 4.5 28.9 0.8 N A:ASN150 4.6 22.9 1.0 HH12 A:ARG254 4.6 29.0 1.0 HH22 A:ARG254 4.7 28.8 1.0 HB3 A:ASN150 4.7 29.7 1.0 HE2 A:HIS281 4.7 27.8 1.0 H A:HIS281 4.8 24.4 1.0 O A:LEU231 4.8 23.1 1.0 H A:HIS151 4.8 28.1 1.0 N A:HIS281 4.8 20.4 1.0 HB3 A:ASP118 4.9 25.4 1.0 HD1 A:HIS199 4.9 23.5 1.0 HE1 A:HIS92 4.9 26.9 1.0 HB3 A:HIS281 4.9 26.6 1.0 CG A:ASP90 4.9 19.7 1.0 O A:HOH566 5.0 23.0 1.0 NE2 A:HIS92 5.0 22.4 1.0 NH1 A:ARG254 5.0 24.1 1.0

R.Hendus-Altenburger, X.Wang, L.M.Sjogaard-Frich, E.Pedraz-Cuesta, S.R.Sheftic, A.H.Bendsoe, R.Page, B.B.Kragelund, S.F.Pedersen, W.Peti. Molecular Basis For the Binding and Selective Dephosphorylation of Na+/H+Exchanger 1 By Calcineurin. Nat Commun V. 10 3489 2019.
ISSN: ESSN 2041-1723
PubMed: 31375679
DOI: 10.1038/S41467-019-11391-7