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Copper in PDB 2gba: Reduced Cu(I) Form at pH 4 of P52G Mutant of Amicyanin

Protein crystallography data

The structure of Reduced Cu(I) Form at pH 4 of P52G Mutant of Amicyanin, PDB code: 2gba was solved by J.K.Ma, C.J.Carrell, F.S.Mathews, V.L.Davidson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 0.92
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 28.450, 56.132, 27.003, 90.00, 96.98, 90.00
R / Rfree (%) 10.8 / 14.8

Copper Binding Sites:

The binding sites of Copper atom in the Reduced Cu(I) Form at pH 4 of P52G Mutant of Amicyanin (pdb code 2gba). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Reduced Cu(I) Form at pH 4 of P52G Mutant of Amicyanin, PDB code: 2gba:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 2gba

Go back to Copper Binding Sites List in 2gba
Copper binding site 1 out of 2 in the Reduced Cu(I) Form at pH 4 of P52G Mutant of Amicyanin


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Reduced Cu(I) Form at pH 4 of P52G Mutant of Amicyanin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu107

b:8.9
occ:0.51
CU A:CU1108 0.7 8.4 0.5
ND1 A:HIS53 2.0 8.7 1.0
ND1 A:HIS95 2.1 9.7 0.5
SG A:CYS92 2.2 9.8 1.0
CE1 A:HIS53 2.9 10.1 1.0
SD A:MET98 2.9 8.9 1.0
CG A:HIS95 3.1 9.1 0.5
CE1 A:HIS95 3.1 10.3 0.5
CD2 A:HIS95 3.1 12.2 0.5
CG A:HIS53 3.1 7.4 1.0
CB A:CYS92 3.2 7.7 1.0
CB A:HIS95 3.4 8.9 0.5
CB A:HIS53 3.6 8.1 1.0
CB A:HIS95 3.6 9.1 0.5
CA A:HIS53 3.7 7.0 1.0
CG A:HIS95 3.7 10.6 0.5
CE A:MET98 3.7 11.6 1.0
O A:GLY52 3.7 10.4 1.0
NE2 A:HIS53 4.1 10.1 1.0
CD2 A:HIS53 4.2 8.8 1.0
CD2 A:HIS95 4.2 10.2 0.5
NE2 A:HIS95 4.2 12.0 0.5
NE2 A:HIS95 4.3 14.0 0.5
CG A:MET98 4.4 9.7 1.0
CG A:PRO94 4.4 8.1 1.0
N A:HIS95 4.5 7.4 1.0
CA A:HIS95 4.5 7.5 1.0
C A:GLY52 4.6 8.8 1.0
N A:HIS53 4.6 6.9 1.0
CA A:CYS92 4.6 6.3 1.0
N A:ASN54 4.6 6.4 1.0
CE A:MET28 4.7 18.6 1.0
C A:HIS53 4.7 6.1 1.0
O A:HIS95 4.8 7.2 1.0
CB A:MET98 5.0 8.8 1.0
CD A:PRO94 5.0 7.5 1.0

Copper binding site 2 out of 2 in 2gba

Go back to Copper Binding Sites List in 2gba
Copper binding site 2 out of 2 in the Reduced Cu(I) Form at pH 4 of P52G Mutant of Amicyanin


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Reduced Cu(I) Form at pH 4 of P52G Mutant of Amicyanin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu108

b:8.4
occ:0.49
CU A:CU1107 0.7 8.9 0.5
ND1 A:HIS53 1.8 8.7 1.0
SG A:CYS92 2.1 9.8 1.0
SD A:MET98 2.8 8.9 1.0
ND1 A:HIS95 2.8 9.7 0.5
CG A:HIS53 2.8 7.4 1.0
CE1 A:HIS53 2.9 10.1 1.0
CB A:CYS92 3.0 7.7 1.0
CB A:HIS53 3.2 8.1 1.0
CE A:MET98 3.3 11.6 1.0
CA A:HIS53 3.4 7.0 1.0
CG A:HIS95 3.7 9.1 0.5
CE1 A:HIS95 3.7 10.3 0.5
CD2 A:HIS95 3.8 12.2 0.5
CB A:HIS95 3.9 8.9 0.5
NE2 A:HIS53 4.0 10.1 1.0
CD2 A:HIS53 4.0 8.8 1.0
O A:GLY52 4.0 10.4 1.0
CB A:HIS95 4.1 9.1 0.5
N A:ASN54 4.3 6.4 1.0
CG A:HIS95 4.3 10.6 0.5
CG A:MET98 4.3 9.7 1.0
C A:HIS53 4.4 6.1 1.0
CA A:CYS92 4.4 6.3 1.0
N A:HIS53 4.5 6.9 1.0
C A:GLY52 4.7 8.8 1.0
CB A:MET98 4.8 8.8 1.0
O A:ASN54 4.8 6.5 1.0
CG A:PRO94 4.9 8.1 1.0
CD2 A:HIS95 4.9 10.2 0.5
NE2 A:HIS95 4.9 12.0 0.5
O A:HIS95 4.9 7.2 1.0
N A:HIS95 5.0 7.4 1.0
CA A:HIS95 5.0 7.5 1.0

Reference:

J.K.Ma, C.J.Carrell, F.S.Mathews, V.L.Davidson. Site-Directed Mutagenesis of Proline 52 to Glycine in Amicyanin Converts A True Electron Transfer Reaction Into One That Is Conformationally Gated. Biochemistry V. 45 8284 2006.
ISSN: ISSN 0006-2960
PubMed: 16819827
DOI: 10.1021/BI0605134
Page generated: Wed Oct 28 14:19:43 2020
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