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Copper in PDB 6xx2: Crystal Structure of the C-Src SH3 Domain H122R-Q128K Mutant in Complex with Cu(II) at pH 7.5 Co-Crystallized with Methyl Beta- Cyclodextrin

Enzymatic activity of Crystal Structure of the C-Src SH3 Domain H122R-Q128K Mutant in Complex with Cu(II) at pH 7.5 Co-Crystallized with Methyl Beta- Cyclodextrin

All present enzymatic activity of Crystal Structure of the C-Src SH3 Domain H122R-Q128K Mutant in Complex with Cu(II) at pH 7.5 Co-Crystallized with Methyl Beta- Cyclodextrin:
2.7.10.2;

Protein crystallography data

The structure of Crystal Structure of the C-Src SH3 Domain H122R-Q128K Mutant in Complex with Cu(II) at pH 7.5 Co-Crystallized with Methyl Beta- Cyclodextrin, PDB code: 6xx2 was solved by A.Camara-Artigas, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.83 / 1.25
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 35.606, 35.606, 81.228, 90.00, 90.00, 120.00
R / Rfree (%) 17.9 / 20.7

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of the C-Src SH3 Domain H122R-Q128K Mutant in Complex with Cu(II) at pH 7.5 Co-Crystallized with Methyl Beta- Cyclodextrin (pdb code 6xx2). 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 Crystal Structure of the C-Src SH3 Domain H122R-Q128K Mutant in Complex with Cu(II) at pH 7.5 Co-Crystallized with Methyl Beta- Cyclodextrin, PDB code: 6xx2:

Copper binding site 1 out of 1 in 6xx2

Go back to Copper Binding Sites List in 6xx2
Copper binding site 1 out of 1 in the Crystal Structure of the C-Src SH3 Domain H122R-Q128K Mutant in Complex with Cu(II) at pH 7.5 Co-Crystallized with Methyl Beta- Cyclodextrin


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Crystal Structure of the C-Src SH3 Domain H122R-Q128K Mutant in Complex with Cu(II) at pH 7.5 Co-Crystallized with Methyl Beta- Cyclodextrin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu201

b:65.4
occ:1.00
 ND1 A:HIS83 1.8 42.7 1.0
N A:SER82 2.0 58.0 1.0
N A:HIS83 2.2 43.9 1.0
CE1 A:HIS83 2.7 45.6 1.0
HE1 A:HIS83 2.9 54.8 1.0
CG A:HIS83 2.9 43.9 1.0
C A:SER82 3.0 52.1 1.0
CA A:SER82 3.0 56.4 1.0
CA A:HIS83 3.2 40.9 1.0
H A:MET84 3.4 39.1 1.0
CB A:HIS83 3.4 42.3 1.0
HG2 A:MET84 3.5 49.9 1.0
HB3 A:HIS83 3.5 50.8 1.0
HA A:SER82 3.7 67.7 1.0
N A:MET84 3.8 32.6 1.0
NE2 A:HIS83 3.8 45.3 1.0
C A:HIS83 3.9 36.3 1.0
CB A:SER82 3.9 56.4 1.0
CD2 A:HIS83 4.0 44.5 1.0
HG3 A:MET84 4.0 49.9 1.0
HA A:HIS83 4.0 49.0 1.0
CG A:MET84 4.1 41.6 1.0
O A:SER82 4.2 54.8 1.0
HB2 A:HIS83 4.3 50.8 1.0
HB2 A:MET84 4.5 41.0 1.0
HE2 A:HIS83 4.6 54.3 1.0
CB A:MET84 4.7 34.2 1.0
HD2 A:HIS83 4.8 53.4 1.0
CA A:MET84 4.9 30.8 1.0
O A:HIS83 4.9 40.9 1.0

Reference:

M.Plaza-Garrido, M.C.Salinas-Garcia, J.C.Martinez, A.Camara-Artigas. The Effect of An Engineered Atcun Motif on the Structure and Biophysical Properties of the SH3 Domain of C-Src Tyrosine Kinase. J.Biol.Inorg.Chem. 2020.
ISSN: ESSN 1432-1327
PubMed: 32279137
DOI: 10.1007/S00775-020-01785-0
Page generated: Wed Jul 31 07:51:13 2024

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