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Copper in PDB 2r27: Constitutively Zinc-Deficient Mutant of Human Superoxide Dismutase (Sod), C6A, H80S, H83S, C111S

Enzymatic activity of Constitutively Zinc-Deficient Mutant of Human Superoxide Dismutase (Sod), C6A, H80S, H83S, C111S

All present enzymatic activity of Constitutively Zinc-Deficient Mutant of Human Superoxide Dismutase (Sod), C6A, H80S, H83S, C111S:
1.15.1.1;

Protein crystallography data

The structure of Constitutively Zinc-Deficient Mutant of Human Superoxide Dismutase (Sod), C6A, H80S, H83S, C111S, PDB code: 2r27 was solved by B.R.Roberts, E.D.Getzoff, P.A.Karplus, J.S.Beckman, J.A.Tainer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.20 / 2.00
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 107.200, 35.900, 68.300, 90.00, 104.80, 90.00
R / Rfree (%) 18.4 / 24.6

Copper Binding Sites:

The binding sites of Copper atom in the Constitutively Zinc-Deficient Mutant of Human Superoxide Dismutase (Sod), C6A, H80S, H83S, C111S (pdb code 2r27). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 3 binding sites of Copper where determined in the Constitutively Zinc-Deficient Mutant of Human Superoxide Dismutase (Sod), C6A, H80S, H83S, C111S, PDB code: 2r27:
Jump to Copper binding site number: 1; 2; 3;

Copper binding site 1 out of 3 in 2r27

Go back to Copper Binding Sites List in 2r27
Copper binding site 1 out of 3 in the Constitutively Zinc-Deficient Mutant of Human Superoxide Dismutase (Sod), C6A, H80S, H83S, C111S


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Constitutively Zinc-Deficient Mutant of Human Superoxide Dismutase (Sod), C6A, H80S, H83S, C111S within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu154

b:29.8
occ:0.83
CU A:CU154 0.0 29.8 0.8
CU A:CU154 1.3 31.3 0.2
NE2 A:HIS48 1.9 30.4 1.0
NE2 A:HIS120 2.2 26.1 1.0
ND1 A:HIS46 2.2 27.4 1.0
NE2 A:HIS63 2.4 35.8 1.0
O A:HOH223 2.7 44.9 1.0
CE1 A:HIS48 2.8 28.8 1.0
CD2 A:HIS48 3.0 20.6 1.0
CD2 A:HIS63 3.1 33.0 1.0
CE1 A:HIS120 3.1 24.2 1.0
CG A:HIS46 3.1 27.6 1.0
CD2 A:HIS120 3.2 23.5 1.0
CE1 A:HIS46 3.2 31.2 1.0
CB A:HIS46 3.4 22.8 1.0
CE1 A:HIS63 3.6 37.6 1.0
ND1 A:HIS48 4.0 26.4 1.0
CG A:HIS48 4.1 22.7 1.0
ND1 A:HIS120 4.2 24.3 1.0
CG A:HIS120 4.2 25.7 1.0
CD2 A:HIS46 4.3 31.3 1.0
NE2 A:HIS46 4.3 27.9 1.0
CG A:HIS63 4.3 32.3 1.0
ND1 A:HIS63 4.5 33.3 1.0
CA A:HIS46 4.6 22.9 1.0
CB A:VAL118 4.6 22.4 1.0
O A:HOH160 4.7 27.9 1.0
CG1 A:VAL118 4.7 22.3 1.0
N A:HIS46 4.7 26.6 1.0

Copper binding site 2 out of 3 in 2r27

Go back to Copper Binding Sites List in 2r27
Copper binding site 2 out of 3 in the Constitutively Zinc-Deficient Mutant of Human Superoxide Dismutase (Sod), C6A, H80S, H83S, C111S


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Constitutively Zinc-Deficient Mutant of Human Superoxide Dismutase (Sod), C6A, H80S, H83S, C111S within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu154

b:31.3
occ:0.17
CU A:CU154 0.0 31.3 0.2
CU A:CU154 1.3 29.8 0.8
NE2 A:HIS120 2.2 26.1 1.0
NE2 A:HIS48 2.2 30.4 1.0
ND1 A:HIS46 2.5 27.4 1.0
CD2 A:HIS48 2.8 20.6 1.0
CD2 A:HIS120 2.8 23.5 1.0
CB A:HIS46 3.0 22.8 1.0
CG A:HIS46 3.0 27.6 1.0
CE1 A:HIS120 3.3 24.2 1.0
CE1 A:HIS48 3.4 28.8 1.0
NE2 A:HIS63 3.5 35.8 1.0
CB A:VAL118 3.5 22.4 1.0
CE1 A:HIS46 3.6 31.2 1.0
N A:HIS46 3.7 26.6 1.0
CG1 A:VAL118 3.8 22.3 1.0
CA A:HIS46 3.8 22.9 1.0
O A:HOH223 4.0 44.9 1.0
CD2 A:HIS63 4.0 33.0 1.0
O A:HIS46 4.1 22.7 1.0
CG A:HIS48 4.1 22.7 1.0
CG A:HIS120 4.1 25.7 1.0
O A:VAL118 4.1 21.4 1.0
C A:HIS46 4.1 26.8 1.0
ND1 A:HIS48 4.3 26.4 1.0
ND1 A:HIS120 4.3 24.3 1.0
CD2 A:HIS46 4.3 31.3 1.0
CG2 A:VAL118 4.3 21.0 1.0
C A:VAL118 4.5 19.3 1.0
NE2 A:HIS46 4.5 27.9 1.0
CE1 A:HIS63 4.6 37.6 1.0
CA A:VAL118 4.6 18.6 1.0
C A:PHE45 4.7 23.0 1.0

Copper binding site 3 out of 3 in 2r27

Go back to Copper Binding Sites List in 2r27
Copper binding site 3 out of 3 in the Constitutively Zinc-Deficient Mutant of Human Superoxide Dismutase (Sod), C6A, H80S, H83S, C111S


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Constitutively Zinc-Deficient Mutant of Human Superoxide Dismutase (Sod), C6A, H80S, H83S, C111S within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu154

b:42.4
occ:1.00
NE2 B:HIS120 2.0 29.0 1.0
ND1 B:HIS46 2.1 33.6 1.0
NE2 B:HIS48 2.2 40.2 1.0
NE2 B:HIS63 2.5 61.3 1.0
O B:HOH234 2.8 52.8 1.0
CE1 B:HIS120 2.9 33.4 1.0
CE1 B:HIS46 3.0 37.5 1.0
CD2 B:HIS120 3.0 30.7 1.0
CG B:HIS46 3.1 35.2 1.0
CD2 B:HIS63 3.1 57.9 1.0
CE1 B:HIS48 3.1 34.4 1.0
CD2 B:HIS48 3.2 27.5 1.0
CB B:HIS46 3.4 32.7 1.0
CE1 B:HIS63 3.7 64.0 1.0
ND1 B:HIS120 4.0 29.9 1.0
CG B:HIS120 4.1 32.5 1.0
NE2 B:HIS46 4.1 34.9 1.0
CD2 B:HIS46 4.2 37.6 1.0
ND1 B:HIS48 4.2 36.0 1.0
CG B:HIS48 4.3 34.6 1.0
CG B:HIS63 4.3 54.7 1.0
ND1 B:HIS63 4.6 59.6 1.0
CA B:HIS46 4.6 28.7 1.0
CG1 B:VAL118 4.7 25.2 1.0
CB B:VAL118 4.7 26.5 1.0
N B:HIS46 4.8 25.6 1.0
O B:HOH193 4.9 53.0 1.0

Reference:

B.R.Roberts, J.A.Tainer, E.D.Getzoff, D.A.Malencik, S.R.Anderson, V.C.Bomben, K.R.Meyers, P.A.Karplus, J.S.Beckman. Structural Characterization of Zinc-Deficient Human Superoxide Dismutase and Implications For Als. J.Mol.Biol. V. 373 877 2007.
ISSN: ISSN 0022-2836
PubMed: 17888947
DOI: 10.1016/J.JMB.2007.07.043
Page generated: Wed Oct 28 14:21:36 2020
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