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Iron in PDB 6nuc: Structure of Calcineurin in Complex with NHE1 Peptide

Enzymatic activity of Structure of Calcineurin in Complex with NHE1 Peptide

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

Protein crystallography data

The structure of Structure of Calcineurin in Complex with NHE1 Peptide, PDB code: 6nuc 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) 37.97 / 1.90
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 79.549, 127.073, 127.421, 90.00, 90.00, 90.00
R / Rfree (%) 16.3 / 19.4

Other elements in 6nuc:

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

Zinc (Zn) 1 atom
Calcium (Ca) 4 atoms
Sodium (Na) 1 atom

Iron Binding Sites:

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

Iron binding site 1 out of 1 in 6nuc

Go back to Iron Binding Sites List in 6nuc
Iron binding site 1 out of 1 in the Structure of Calcineurin in Complex with NHE1 Peptide


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Calcineurin in Complex with NHE1 Peptide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe401

b:23.8
occ:0.53
O A:HOH525 1.9 27.5 1.0
OD2 A:ASP90 2.1 23.7 1.0
NE2 A:HIS92 2.1 23.8 1.0
O4 A:PO4403 2.1 25.5 0.8
OD2 A:ASP118 2.2 20.7 1.0
O A:HOH621 2.2 24.2 1.0
CE1 A:HIS92 3.0 21.1 1.0
CD2 A:HIS92 3.1 20.8 1.0
HE1 A:HIS92 3.2 25.3 1.0
CG A:ASP118 3.2 21.1 1.0
CG A:ASP90 3.2 22.9 1.0
ZN A:ZN402 3.3 22.1 0.8
HB3 A:ASP118 3.3 24.7 1.0
P A:PO4403 3.3 28.9 0.8
HD2 A:HIS92 3.3 25.0 1.0
O1 A:PO4403 3.5 22.6 0.8
HH22 A:ARG122 3.6 38.9 1.0
HB3 A:ASP90 3.6 24.0 1.0
CB A:ASP118 3.6 20.6 1.0
HB2 A:ASP118 3.8 24.7 1.0
HA A:HIS281 3.8 28.1 1.0
HE1 A:HIS199 3.8 24.4 1.0
HE1 A:PHE306 3.9 28.1 1.0
O2 A:PO4403 3.9 28.7 0.8
CB A:ASP90 4.0 20.0 1.0
HD2 A:HIS151 4.0 30.5 1.0
O A:HOH519 4.1 32.4 1.0
OD1 A:ASP90 4.1 21.9 1.0
ND1 A:HIS92 4.2 21.1 1.0
CG A:HIS92 4.2 20.6 1.0
NH2 A:ARG122 4.2 32.4 1.0
HH21 A:ARG122 4.3 38.9 1.0
OD1 A:ASP118 4.3 20.7 1.0
HB2 A:ASP90 4.4 24.0 1.0
CE1 A:HIS199 4.4 20.3 1.0
NE2 A:HIS199 4.4 18.8 1.0
CD2 A:HIS151 4.5 25.4 1.0
OH A:TYR311 4.5 28.5 1.0
O A:HIS281 4.5 22.6 1.0
O3 A:PO4403 4.5 29.9 0.8
HE2 A:HIS151 4.6 28.3 1.0
HH A:TYR311 4.7 34.2 1.0
CA A:HIS281 4.7 23.4 1.0
NE2 A:HIS151 4.8 23.6 1.0
CE1 A:PHE306 4.8 23.4 1.0
H A:HIS281 4.8 24.9 1.0
C A:HIS281 4.8 21.5 1.0
OD1 A:ASN150 4.9 21.9 1.0
ND1 A:HIS281 4.9 23.8 1.0
HD1 A:HIS92 4.9 25.3 1.0

Reference:

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
Page generated: Wed Aug 7 04:00:27 2024

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