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Copper in PDB 3kh3: Crystal Structure of Human Cu/Zn Superoxide Dismutase Recombinantly Produced in Leishmania Tarantolae; P212121 Crystal Form Containing 12 Chains in the Asymmetric Unit

Enzymatic activity of Crystal Structure of Human Cu/Zn Superoxide Dismutase Recombinantly Produced in Leishmania Tarantolae; P212121 Crystal Form Containing 12 Chains in the Asymmetric Unit

All present enzymatic activity of Crystal Structure of Human Cu/Zn Superoxide Dismutase Recombinantly Produced in Leishmania Tarantolae; P212121 Crystal Form Containing 12 Chains in the Asymmetric Unit:
1.15.1.1;

Protein crystallography data

The structure of Crystal Structure of Human Cu/Zn Superoxide Dismutase Recombinantly Produced in Leishmania Tarantolae; P212121 Crystal Form Containing 12 Chains in the Asymmetric Unit, PDB code: 3kh3 was solved by E.M.Gazdag, W.Blankenfeldt, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.78 / 3.50
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 75.500, 166.610, 174.980, 90.00, 90.00, 90.00
R / Rfree (%) 24.3 / 27.7

Other elements in 3kh3:

The structure of Crystal Structure of Human Cu/Zn Superoxide Dismutase Recombinantly Produced in Leishmania Tarantolae; P212121 Crystal Form Containing 12 Chains in the Asymmetric Unit also contains other interesting chemical elements:

Zinc (Zn) 12 atoms

Copper Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 12;

Binding sites:

The binding sites of Copper atom in the Crystal Structure of Human Cu/Zn Superoxide Dismutase Recombinantly Produced in Leishmania Tarantolae; P212121 Crystal Form Containing 12 Chains in the Asymmetric Unit (pdb code 3kh3). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 12 binding sites of Copper where determined in the Crystal Structure of Human Cu/Zn Superoxide Dismutase Recombinantly Produced in Leishmania Tarantolae; P212121 Crystal Form Containing 12 Chains in the Asymmetric Unit, PDB code: 3kh3:
Jump to Copper binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Copper binding site 1 out of 12 in 3kh3

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Copper binding site 1 out of 12 in the Crystal Structure of Human Cu/Zn Superoxide Dismutase Recombinantly Produced in Leishmania Tarantolae; P212121 Crystal Form Containing 12 Chains in the Asymmetric Unit


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 Human Cu/Zn Superoxide Dismutase Recombinantly Produced in Leishmania Tarantolae; P212121 Crystal Form Containing 12 Chains in the Asymmetric Unit within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu155

b:58.3
occ:1.00
NE2 A:HIS49 2.4 42.8 1.0
NE2 A:HIS121 2.4 45.7 1.0
ND1 A:HIS47 2.4 46.5 1.0
NE2 A:HIS64 3.0 48.2 1.0
CE1 A:HIS49 3.1 43.6 1.0
CG A:HIS47 3.2 46.1 1.0
CE1 A:HIS121 3.2 47.3 1.0
CD2 A:HIS121 3.2 45.9 1.0
CB A:HIS47 3.3 44.6 1.0
CD2 A:HIS49 3.4 41.7 1.0
CE1 A:HIS47 3.5 48.6 1.0
CD2 A:HIS64 3.5 47.5 1.0
CE1 A:HIS64 3.7 49.2 1.0
ND1 A:HIS121 4.1 48.8 1.0
CG A:HIS121 4.2 47.9 1.0
ND1 A:HIS49 4.3 43.0 1.0
CD2 A:HIS47 4.3 48.5 1.0
CA A:HIS47 4.4 43.9 1.0
CG A:HIS64 4.4 48.1 1.0
CG A:HIS49 4.4 41.9 1.0
NE2 A:HIS47 4.4 49.7 1.0
CG1 A:VAL119 4.4 42.7 1.0
N A:HIS47 4.5 44.4 1.0
ND1 A:HIS64 4.5 49.0 1.0
CB A:VAL119 4.6 41.2 1.0
O A:VAL119 4.8 43.5 1.0
C A:HIS47 4.9 42.4 1.0
O A:HIS47 4.9 41.6 1.0

Copper binding site 2 out of 12 in 3kh3

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Copper binding site 2 out of 12 in the Crystal Structure of Human Cu/Zn Superoxide Dismutase Recombinantly Produced in Leishmania Tarantolae; P212121 Crystal Form Containing 12 Chains in the Asymmetric Unit


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Crystal Structure of Human Cu/Zn Superoxide Dismutase Recombinantly Produced in Leishmania Tarantolae; P212121 Crystal Form Containing 12 Chains in the Asymmetric Unit within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu155

b:46.5
occ:1.00
NE2 B:HIS121 2.3 34.0 1.0
ND1 B:HIS47 2.3 31.9 1.0
NE2 B:HIS49 2.4 34.7 1.0
NE2 B:HIS64 3.0 36.1 1.0
CG B:HIS47 3.1 31.5 1.0
CD2 B:HIS121 3.1 33.0 1.0
CE1 B:HIS121 3.1 35.5 1.0
CB B:HIS47 3.2 31.7 1.0
CE1 B:HIS49 3.3 36.5 1.0
CE1 B:HIS47 3.3 32.2 1.0
CD2 B:HIS49 3.5 34.1 1.0
CD2 B:HIS64 3.6 37.0 1.0
CE1 B:HIS64 3.7 35.8 1.0
ND1 B:HIS121 4.0 35.6 1.0
CG B:HIS121 4.1 34.0 1.0
CD2 B:HIS47 4.2 32.0 1.0
CA B:HIS47 4.3 30.9 1.0
NE2 B:HIS47 4.3 32.0 1.0
ND1 B:HIS49 4.4 37.1 1.0
N B:HIS47 4.4 30.5 1.0
CG1 B:VAL119 4.4 33.8 1.0
CG B:HIS64 4.5 37.1 1.0
CG B:HIS49 4.5 35.9 1.0
ND1 B:HIS64 4.5 36.1 1.0
CB B:VAL119 4.7 32.9 1.0
O B:VAL119 4.7 31.3 1.0
O B:HIS47 4.8 31.3 1.0
C B:HIS47 4.8 31.2 1.0
O1 B:SO4157 4.8 0.9 1.0
O2 B:SO4157 5.0 0.1 1.0

Copper binding site 3 out of 12 in 3kh3

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Copper binding site 3 out of 12 in the Crystal Structure of Human Cu/Zn Superoxide Dismutase Recombinantly Produced in Leishmania Tarantolae; P212121 Crystal Form Containing 12 Chains in the Asymmetric Unit


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Crystal Structure of Human Cu/Zn Superoxide Dismutase Recombinantly Produced in Leishmania Tarantolae; P212121 Crystal Form Containing 12 Chains in the Asymmetric Unit within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cu155

b:72.1
occ:1.00
ND1 C:HIS47 2.0 54.9 1.0
NE2 C:HIS121 2.5 65.2 1.0
NE2 C:HIS49 2.8 65.1 1.0
CG C:HIS47 2.8 53.0 1.0
NE2 C:HIS64 2.9 56.4 1.0
CE1 C:HIS47 3.0 53.4 1.0
CB C:HIS47 3.1 54.8 1.0
CD2 C:HIS121 3.2 64.5 1.0
CE1 C:HIS121 3.2 66.5 1.0
CE1 C:HIS64 3.5 53.4 1.0
CE1 C:HIS49 3.5 67.4 1.0
CD2 C:HIS64 3.5 57.8 1.0
CD2 C:HIS49 3.7 64.9 1.0
CD2 C:HIS47 3.9 51.0 1.0
NE2 C:HIS47 4.0 51.0 1.0
ND1 C:HIS121 4.1 66.8 1.0
CG C:HIS121 4.1 65.5 1.0
CA C:HIS47 4.2 55.9 1.0
ND1 C:HIS64 4.3 52.7 1.0
N C:HIS47 4.3 56.9 1.0
CG C:HIS64 4.4 55.5 1.0
ND1 C:HIS49 4.7 69.0 1.0
CG1 C:VAL119 4.7 72.5 1.0
O C:VAL119 4.8 65.6 1.0
CG C:HIS49 4.8 67.6 1.0
C C:HIS47 4.9 58.6 1.0
O C:HIS47 4.9 61.8 1.0
CB C:VAL119 4.9 71.0 1.0
O C:THR138 5.0 55.6 1.0

Copper binding site 4 out of 12 in 3kh3

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Copper binding site 4 out of 12 in the Crystal Structure of Human Cu/Zn Superoxide Dismutase Recombinantly Produced in Leishmania Tarantolae; P212121 Crystal Form Containing 12 Chains in the Asymmetric Unit


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Crystal Structure of Human Cu/Zn Superoxide Dismutase Recombinantly Produced in Leishmania Tarantolae; P212121 Crystal Form Containing 12 Chains in the Asymmetric Unit within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cu155

b:0.4
occ:1.00
NE2 D:HIS49 2.1 0.2 1.0
CD2 D:HIS49 2.6 0.6 1.0
O D:VAL119 2.9 0.2 1.0
NE2 D:HIS121 3.1 0.3 1.0
CB D:HIS47 3.2 0.2 1.0
CE1 D:HIS49 3.3 0.3 1.0
CB D:VAL119 3.3 0.8 1.0
C D:HIS47 3.6 0.4 1.0
CA D:HIS47 3.6 0.1 1.0
N D:HIS47 3.7 0.1 1.0
C D:VAL119 3.8 0.2 1.0
CG1 D:VAL119 3.8 1.0 1.0
CG D:HIS49 3.8 0.7 1.0
O D:HIS47 3.8 0.8 1.0
CE1 D:HIS64 3.9 0.2 1.0
CE1 D:HIS121 3.9 0.0 1.0
CA D:VAL119 3.9 0.3 1.0
N D:VAL48 4.0 0.8 1.0
CD2 D:HIS121 4.0 0.3 1.0
N D:VAL119 4.0 0.8 1.0
NE2 D:HIS64 4.1 0.8 1.0
ND1 D:HIS49 4.1 0.1 1.0
CG D:HIS47 4.2 0.6 1.0
ND1 D:HIS47 4.2 0.1 1.0
CG2 D:VAL119 4.4 0.6 1.0
ND1 D:HIS64 4.4 0.1 1.0
CA D:VAL48 4.6 0.7 1.0
C D:VAL48 4.6 0.0 1.0
CD2 D:HIS64 4.8 0.7 1.0
O D:THR117 4.8 0.3 1.0
N D:HIS49 4.9 0.9 1.0
O D:VAL48 4.9 0.0 1.0
ND1 D:HIS121 5.0 0.7 1.0
CG D:HIS64 5.0 0.5 1.0
C D:PHE46 5.0 0.1 1.0

Copper binding site 5 out of 12 in 3kh3

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Copper binding site 5 out of 12 in the Crystal Structure of Human Cu/Zn Superoxide Dismutase Recombinantly Produced in Leishmania Tarantolae; P212121 Crystal Form Containing 12 Chains in the Asymmetric Unit


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 5 of Crystal Structure of Human Cu/Zn Superoxide Dismutase Recombinantly Produced in Leishmania Tarantolae; P212121 Crystal Form Containing 12 Chains in the Asymmetric Unit within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Cu155

b:0.3
occ:1.00
ND1 E:HIS47 2.3 0.8 1.0
NE2 E:HIS49 2.5 0.3 1.0
NE2 E:HIS121 2.6 0.7 1.0
NE2 E:HIS64 2.8 0.3 1.0
CG E:HIS47 2.9 0.9 1.0
CB E:HIS47 3.0 0.1 1.0
CE1 E:HIS49 3.2 0.3 1.0
CE1 E:HIS47 3.3 0.3 1.0
CD2 E:HIS121 3.3 0.7 1.0
CE1 E:HIS121 3.4 0.3 1.0
CD2 E:HIS64 3.4 0.7 1.0
CD2 E:HIS49 3.4 97.8 1.0
CE1 E:HIS64 3.5 0.7 1.0
CD2 E:HIS47 4.1 0.4 1.0
NE2 E:HIS47 4.2 0.8 1.0
CA E:HIS47 4.2 99.4 1.0
CG E:HIS64 4.2 0.7 1.0
ND1 E:HIS64 4.2 0.4 1.0
CG E:HIS121 4.3 0.8 1.0
ND1 E:HIS121 4.3 0.7 1.0
ND1 E:HIS49 4.3 0.5 1.0
N E:HIS47 4.4 0.3 1.0
CG E:HIS49 4.5 97.5 1.0
CG1 E:VAL119 4.6 1.0 1.0
C E:HIS47 4.7 95.3 1.0
CB E:VAL119 4.8 98.2 1.0
O E:HIS47 4.8 94.3 1.0
O E:VAL119 4.8 0.7 1.0

Copper binding site 6 out of 12 in 3kh3

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Copper binding site 6 out of 12 in the Crystal Structure of Human Cu/Zn Superoxide Dismutase Recombinantly Produced in Leishmania Tarantolae; P212121 Crystal Form Containing 12 Chains in the Asymmetric Unit


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 6 of Crystal Structure of Human Cu/Zn Superoxide Dismutase Recombinantly Produced in Leishmania Tarantolae; P212121 Crystal Form Containing 12 Chains in the Asymmetric Unit within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Cu155

b:53.5
occ:1.00
NE2 F:HIS121 2.2 41.5 1.0
ND1 F:HIS47 2.3 37.6 1.0
NE2 F:HIS49 2.5 43.5 1.0
CD2 F:HIS121 3.0 40.7 1.0
CG F:HIS47 3.0 37.2 1.0
CE1 F:HIS121 3.1 42.4 1.0
CB F:HIS47 3.1 38.5 1.0
NE2 F:HIS64 3.2 40.5 1.0
CE1 F:HIS47 3.3 36.9 1.0
CE1 F:HIS49 3.3 45.3 1.0
CD2 F:HIS49 3.5 43.9 1.0
CD2 F:HIS64 3.7 42.0 1.0
CE1 F:HIS64 3.8 39.4 1.0
CG F:HIS121 4.0 41.0 1.0
ND1 F:HIS121 4.0 42.1 1.0
CD2 F:HIS47 4.2 36.9 1.0
CA F:HIS47 4.2 38.8 1.0
N F:HIS47 4.3 38.7 1.0
NE2 F:HIS47 4.3 36.3 1.0
CG1 F:VAL119 4.3 45.1 1.0
ND1 F:HIS49 4.5 46.9 1.0
CB F:VAL119 4.5 44.8 1.0
CG F:HIS49 4.6 46.1 1.0
O F:VAL119 4.6 42.0 1.0
CG F:HIS64 4.6 41.8 1.0
ND1 F:HIS64 4.6 39.9 1.0
O F:HIS47 4.7 41.6 1.0
C F:HIS47 4.7 40.4 1.0

Copper binding site 7 out of 12 in 3kh3

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Copper binding site 7 out of 12 in the Crystal Structure of Human Cu/Zn Superoxide Dismutase Recombinantly Produced in Leishmania Tarantolae; P212121 Crystal Form Containing 12 Chains in the Asymmetric Unit


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 7 of Crystal Structure of Human Cu/Zn Superoxide Dismutase Recombinantly Produced in Leishmania Tarantolae; P212121 Crystal Form Containing 12 Chains in the Asymmetric Unit within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Cu155

b:78.4
occ:1.00
ND1 G:HIS47 2.2 68.3 1.0
NE2 G:HIS121 2.3 66.9 1.0
NE2 G:HIS49 2.8 61.8 1.0
NE2 G:HIS64 2.9 66.3 1.0
CG G:HIS47 3.0 67.7 1.0
CE1 G:HIS121 3.0 68.2 1.0
CD2 G:HIS121 3.1 68.5 1.0
CE1 G:HIS47 3.1 70.8 1.0
CB G:HIS47 3.3 65.6 1.0
CE1 G:HIS49 3.5 61.2 1.0
CD2 G:HIS64 3.5 64.7 1.0
CE1 G:HIS64 3.6 67.7 1.0
CD2 G:HIS49 3.8 60.4 1.0
ND1 G:HIS121 3.9 70.8 1.0
CG G:HIS121 4.0 71.0 1.0
CD2 G:HIS47 4.1 70.2 1.0
NE2 G:HIS47 4.1 72.0 1.0
ND1 G:HIS64 4.4 67.0 1.0
CG G:HIS64 4.4 65.2 1.0
CA G:HIS47 4.5 65.9 1.0
N G:HIS47 4.5 67.7 1.0
CG1 G:VAL119 4.6 64.6 1.0
ND1 G:HIS49 4.7 59.7 1.0
CG G:HIS49 4.8 59.3 1.0
O G:VAL119 4.8 67.4 1.0
CB G:VAL119 4.9 63.0 1.0
O G:THR138 5.0 72.8 1.0

Copper binding site 8 out of 12 in 3kh3

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Copper binding site 8 out of 12 in the Crystal Structure of Human Cu/Zn Superoxide Dismutase Recombinantly Produced in Leishmania Tarantolae; P212121 Crystal Form Containing 12 Chains in the Asymmetric Unit


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 8 of Crystal Structure of Human Cu/Zn Superoxide Dismutase Recombinantly Produced in Leishmania Tarantolae; P212121 Crystal Form Containing 12 Chains in the Asymmetric Unit within 5.0Å range:
probe atom residue distance (Å) B Occ
H:Cu155

b:58.0
occ:1.00
ND1 H:HIS47 2.3 41.8 1.0
NE2 H:HIS121 2.4 46.9 1.0
NE2 H:HIS49 2.6 47.4 1.0
NE2 H:HIS64 2.9 46.6 1.0
CG H:HIS47 3.0 40.4 1.0
CE1 H:HIS121 3.1 49.0 1.0
CD2 H:HIS121 3.1 45.4 1.0
CB H:HIS47 3.2 40.7 1.0
CE1 H:HIS47 3.3 41.7 1.0
CE1 H:HIS49 3.3 50.2 1.0
CD2 H:HIS64 3.5 47.8 1.0
CD2 H:HIS49 3.6 46.6 1.0
CE1 H:HIS64 3.6 45.0 1.0
ND1 H:HIS121 4.0 48.9 1.0
CG H:HIS121 4.1 46.6 1.0
CD2 H:HIS47 4.2 40.2 1.0
NE2 H:HIS47 4.3 40.7 1.0
CA H:HIS47 4.3 39.5 1.0
CG H:HIS64 4.4 47.0 1.0
N H:HIS47 4.4 39.2 1.0
ND1 H:HIS64 4.4 45.1 1.0
ND1 H:HIS49 4.5 51.3 1.0
CG1 H:VAL119 4.5 47.8 1.0
CG H:HIS49 4.6 49.2 1.0
CB H:VAL119 4.8 46.2 1.0
O H:VAL119 4.8 42.2 1.0
C H:HIS47 4.9 40.4 1.0
O H:HIS47 4.9 41.3 1.0

Copper binding site 9 out of 12 in 3kh3

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Copper binding site 9 out of 12 in the Crystal Structure of Human Cu/Zn Superoxide Dismutase Recombinantly Produced in Leishmania Tarantolae; P212121 Crystal Form Containing 12 Chains in the Asymmetric Unit


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 9 of Crystal Structure of Human Cu/Zn Superoxide Dismutase Recombinantly Produced in Leishmania Tarantolae; P212121 Crystal Form Containing 12 Chains in the Asymmetric Unit within 5.0Å range:
probe atom residue distance (Å) B Occ
I:Cu155

b:59.4
occ:1.00
ND1 I:HIS47 2.3 47.2 1.0
NE2 I:HIS121 2.4 46.2 1.0
NE2 I:HIS49 2.6 44.0 1.0
NE2 I:HIS64 3.0 49.0 1.0
CG I:HIS47 3.0 46.9 1.0
CD2 I:HIS121 3.1 46.4 1.0
CE1 I:HIS121 3.1 47.7 1.0
CB I:HIS47 3.2 45.4 1.0
CE1 I:HIS47 3.2 49.0 1.0
CE1 I:HIS49 3.4 44.7 1.0
CD2 I:HIS64 3.6 48.5 1.0
CD2 I:HIS49 3.6 42.9 1.0
CE1 I:HIS64 3.7 50.0 1.0
ND1 I:HIS121 4.0 48.9 1.0
CG I:HIS121 4.0 48.1 1.0
CD2 I:HIS47 4.2 49.1 1.0
NE2 I:HIS47 4.2 50.1 1.0
CA I:HIS47 4.4 44.9 1.0
N I:HIS47 4.4 45.3 1.0
CG I:HIS64 4.5 49.0 1.0
ND1 I:HIS64 4.5 49.8 1.0
CG1 I:VAL119 4.5 43.7 1.0
ND1 I:HIS49 4.5 44.2 1.0
CG I:HIS49 4.7 43.1 1.0
O I:VAL119 4.7 44.4 1.0
CB I:VAL119 4.7 42.4 1.0
C I:HIS47 4.9 43.4 1.0
O I:HIS47 4.9 42.9 1.0

Copper binding site 10 out of 12 in 3kh3

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Copper binding site 10 out of 12 in the Crystal Structure of Human Cu/Zn Superoxide Dismutase Recombinantly Produced in Leishmania Tarantolae; P212121 Crystal Form Containing 12 Chains in the Asymmetric Unit


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 10 of Crystal Structure of Human Cu/Zn Superoxide Dismutase Recombinantly Produced in Leishmania Tarantolae; P212121 Crystal Form Containing 12 Chains in the Asymmetric Unit within 5.0Å range:
probe atom residue distance (Å) B Occ
J:Cu155

b:46.7
occ:1.00
ND1 J:HIS47 2.2 32.8 1.0
NE2 J:HIS121 2.4 34.2 1.0
NE2 J:HIS49 2.6 34.4 1.0
CG J:HIS47 2.9 32.5 1.0
NE2 J:HIS64 2.9 36.7 1.0
CB J:HIS47 3.1 32.4 1.0
CD2 J:HIS121 3.1 33.3 1.0
CE1 J:HIS121 3.2 35.7 1.0
CE1 J:HIS47 3.2 33.5 1.0
CE1 J:HIS49 3.4 36.2 1.0
CD2 J:HIS49 3.5 33.9 1.0
CD2 J:HIS64 3.6 37.4 1.0
CE1 J:HIS64 3.6 36.5 1.0
CD2 J:HIS47 4.1 33.5 1.0
CG J:HIS121 4.1 34.3 1.0
ND1 J:HIS121 4.1 35.9 1.0
NE2 J:HIS47 4.2 33.8 1.0
CA J:HIS47 4.3 31.7 1.0
N J:HIS47 4.4 31.3 1.0
ND1 J:HIS64 4.4 36.9 1.0
CG J:HIS64 4.4 37.5 1.0
ND1 J:HIS49 4.5 36.9 1.0
CG1 J:VAL119 4.6 33.3 1.0
CG J:HIS49 4.6 35.5 1.0
O J:VAL119 4.7 31.4 1.0
CB J:VAL119 4.8 32.4 1.0
C J:HIS47 4.8 31.7 1.0
O J:HIS47 4.8 31.6 1.0

Reference:

E.M.Gazdag, I.C.Cirstea, R.Breitling, J.Lukes, W.Blankenfeldt, K.Alexandrov. Purification and Crystallization of Human Cu/Zn Superoxide Dismutase Recombinantly Produced in the Protozoan Leishmania Tarentolae. Acta Crystallogr.,Sect.F V. 66 871 2010.
ISSN: ESSN 1744-3091
PubMed: 20693657
DOI: 10.1107/S1744309110019330
Page generated: Sun Dec 13 11:10:23 2020

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