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Copper in PDB 7nxx: Structure of Superoxide Dismutase 1 (SOD1) in Complex with Nanobody 2 (NB2).

Enzymatic activity of Structure of Superoxide Dismutase 1 (SOD1) in Complex with Nanobody 2 (NB2).

All present enzymatic activity of Structure of Superoxide Dismutase 1 (SOD1) in Complex with Nanobody 2 (NB2).:
1.15.1.1;

Protein crystallography data

The structure of Structure of Superoxide Dismutase 1 (SOD1) in Complex with Nanobody 2 (NB2)., PDB code: 7nxx was solved by R.Gallardo, F.Rousseau, J.Schymkowitz, C.Ulens, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 57.92 / 2.19
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 115.83, 115.83, 83.79, 90, 90, 90
R / Rfree (%) 20.2 / 24.6

Other elements in 7nxx:

The structure of Structure of Superoxide Dismutase 1 (SOD1) in Complex with Nanobody 2 (NB2). also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Copper Binding Sites:

The binding sites of Copper atom in the Structure of Superoxide Dismutase 1 (SOD1) in Complex with Nanobody 2 (NB2). (pdb code 7nxx). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total only one binding site of Copper was determined in the Structure of Superoxide Dismutase 1 (SOD1) in Complex with Nanobody 2 (NB2)., PDB code: 7nxx:

Copper binding site 1 out of 1 in 7nxx

Go back to Copper Binding Sites List in 7nxx
Copper binding site 1 out of 1 in the Structure of Superoxide Dismutase 1 (SOD1) in Complex with Nanobody 2 (NB2).


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Structure of Superoxide Dismutase 1 (SOD1) in Complex with Nanobody 2 (NB2). within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu201

b:43.0
occ:0.78
 NE2 A:HIS48 2.1 48.2 1.0
ND1 A:HIS46 2.1 49.0 1.0
NE2 A:HIS120 2.1 51.9 1.0
CD2 A:HIS120 2.9 50.1 1.0
CE1 A:HIS48 2.9 46.9 1.0
CE1 A:HIS46 3.0 53.1 1.0
CE1 A:HIS63 3.1 72.2 1.0
CD2 A:HIS48 3.2 46.6 1.0
CG A:HIS46 3.2 48.8 1.0
CE1 A:HIS120 3.3 60.3 1.0
ND1 A:HIS63 3.6 73.1 1.0
CB A:HIS46 3.6 49.9 1.0
ND1 A:HIS48 4.1 47.4 1.0
CG A:HIS120 4.1 53.5 1.0
NE2 A:HIS63 4.1 61.3 1.0
NE2 A:HIS46 4.1 49.8 1.0
CG A:HIS48 4.2 40.2 1.0
ND1 A:HIS120 4.3 56.3 1.0
CD2 A:HIS46 4.3 49.5 1.0
CB A:VAL118 4.3 40.9 1.0
N A:HIS46 4.3 46.7 1.0
CG1 A:VAL118 4.4 40.2 1.0
CA A:HIS46 4.5 46.4 1.0
O A:HIS46 4.7 53.5 1.0
O A:VAL118 4.7 60.8 1.0
C A:HIS46 4.8 47.7 1.0
CG A:HIS63 4.8 65.6 1.0

Reference:

R.Van Der Kant, R.Gallardo, E.Michiels, H.Wilkinson, F.Claes, A.Laird, L.Van Den Bosch, W.Robberecht, G.H.Ghassabeh, M.Oliveberg, C.Ulens, J.Schymkowitz, F.Rousseau. Identification and Rational Improvement of A Nanobody That Suppresses Aggregation of Mutant SOD1 To Be Published.
Page generated: Wed Jul 31 08:39:46 2024

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