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Copper in PDB 9ggo: Strand-Swapped Dimer of Engineered Copper Binding SH3-Like Protein

Protein crystallography data

The structure of Strand-Swapped Dimer of Engineered Copper Binding SH3-Like Protein, PDB code: 9ggo was solved by M.Schwan, J.Kopp, I.Sinning, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 37.61 / 2.00
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 56.509, 56.509, 58.778, 90, 90, 120
R / Rfree (%) 20.3 / 22.7

Copper Binding Sites:

The binding sites of Copper atom in the Strand-Swapped Dimer of Engineered Copper Binding SH3-Like Protein (pdb code 9ggo). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Strand-Swapped Dimer of Engineered Copper Binding SH3-Like Protein, PDB code: 9ggo:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 9ggo

Go back to Copper Binding Sites List in 9ggo
Copper binding site 1 out of 2 in the Strand-Swapped Dimer of Engineered Copper Binding SH3-Like Protein


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Strand-Swapped Dimer of Engineered Copper Binding SH3-Like Protein within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu101

b:75.4
occ:1.00
NE2 A:HIS10 2.1 49.0 1.0
NE2 A:HIS13 2.1 52.5 1.0
CE1 A:HIS10 2.9 44.3 1.0
CD2 A:HIS13 3.1 49.4 1.0
CE1 A:HIS13 3.2 56.9 1.0
CD2 A:HIS10 3.2 34.7 1.0
CU A:CU102 3.6 160.3 1.0
CD2 A:HIS50 3.8 48.3 1.0
O A:HOH211 3.9 54.2 1.0
NE2 A:HIS50 4.1 56.3 1.0
ND1 A:HIS10 4.1 47.4 1.0
O A:HOH205 4.2 40.9 1.0
CG A:HIS10 4.2 36.4 1.0
ND1 A:HIS13 4.3 47.0 1.0
CG A:HIS13 4.3 45.2 1.0
O A:THR11 4.5 45.1 1.0

Copper binding site 2 out of 2 in 9ggo

Go back to Copper Binding Sites List in 9ggo
Copper binding site 2 out of 2 in the Strand-Swapped Dimer of Engineered Copper Binding SH3-Like Protein


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Strand-Swapped Dimer of Engineered Copper Binding SH3-Like Protein within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu102

b:160.3
occ:1.00
NE2 A:HIS50 2.1 56.3 1.0
OE1 A:GLU15 2.5 106.5 1.0
CD A:GLU15 2.9 82.7 1.0
CE1 A:HIS50 3.0 49.4 1.0
OE2 A:GLU15 3.1 114.2 1.0
CD2 A:HIS50 3.2 48.3 1.0
CU A:CU101 3.6 75.4 1.0
CE1 A:HIS13 3.7 56.9 1.0
NE2 A:HIS13 4.0 52.5 1.0
CG A:GLU15 4.0 73.2 1.0
ND1 A:HIS50 4.1 46.8 1.0
CG A:HIS50 4.2 42.5 1.0
CD2 A:LEU36 4.8 47.2 1.0
ND1 A:HIS13 4.9 47.0 1.0

Reference:

F.Haege, M.Schwan, M.R.Conde Gonzalec, J.Huber, S.Germer, M.Macri, J.Kopp, I.Sinning, F.Thomas. Strand-Swapped SH3 Domain Dimer with Superoxide Dismutase Activity Acs Central Science 2025.
DOI: 10.1021/ACSCENTSCI.4C01347
Page generated: Mon Jul 14 09:56:06 2025

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