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Copper in PDB 1sda: Crystal Structure of Peroxynitrite-Modified Bovine Cu,Zn Superoxide Dismutase

Enzymatic activity of Crystal Structure of Peroxynitrite-Modified Bovine Cu,Zn Superoxide Dismutase

All present enzymatic activity of Crystal Structure of Peroxynitrite-Modified Bovine Cu,Zn Superoxide Dismutase:
1.15.1.1;

Protein crystallography data

The structure of Crystal Structure of Peroxynitrite-Modified Bovine Cu,Zn Superoxide Dismutase, PDB code: 1sda was solved by C.D.Smith, M.Carson, M.Van Der Woerd, J.Chen, H.Ischiropoulos, J.S.Beckman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 2.50
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 93.650, 90.330, 71.650, 90.00, 95.10, 90.00
R / Rfree (%) 18.7 / n/a

Other elements in 1sda:

The structure of Crystal Structure of Peroxynitrite-Modified Bovine Cu,Zn Superoxide Dismutase also contains other interesting chemical elements:

Zinc (Zn) 4 atoms

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of Peroxynitrite-Modified Bovine Cu,Zn Superoxide Dismutase (pdb code 1sda). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 4 binding sites of Copper where determined in the Crystal Structure of Peroxynitrite-Modified Bovine Cu,Zn Superoxide Dismutase, PDB code: 1sda:
Jump to Copper binding site number: 1; 2; 3; 4;

Copper binding site 1 out of 4 in 1sda

Go back to Copper Binding Sites List in 1sda
Copper binding site 1 out of 4 in the Crystal Structure of Peroxynitrite-Modified Bovine Cu,Zn Superoxide Dismutase


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 Peroxynitrite-Modified Bovine Cu,Zn Superoxide Dismutase within 5.0Å range:
probe atom residue distance (Å) B Occ
O:Cu801

b:17.9
occ:1.00
ND1 O:HIS44 2.0 5.3 1.0
NE2 O:HIS118 2.1 7.1 1.0
NE2 O:HIS46 2.2 10.1 1.0
NE2 O:HIS61 2.4 2.0 1.0
CG O:HIS44 2.6 6.0 1.0
CB O:HIS44 2.7 6.1 1.0
CD2 O:HIS118 2.9 9.1 1.0
CD2 O:HIS61 3.1 2.0 1.0
CE1 O:HIS46 3.1 9.6 1.0
CE1 O:HIS44 3.1 3.4 1.0
CD2 O:HIS46 3.2 7.8 1.0
CE1 O:HIS118 3.2 7.6 1.0
CE1 O:HIS61 3.4 3.8 1.0
CD2 O:HIS44 3.9 5.5 1.0
CG O:HIS118 4.1 7.5 1.0
NE2 O:HIS44 4.1 6.3 1.0
CA O:HIS44 4.1 6.1 1.0
ND1 O:HIS118 4.2 6.7 1.0
ND1 O:HIS46 4.2 8.1 1.0
CG O:HIS61 4.3 2.7 1.0
CG O:HIS46 4.3 8.3 1.0
ND1 O:HIS61 4.4 3.1 1.0
N O:HIS44 4.5 7.6 1.0
CB O:VAL116 4.7 7.4 1.0
C O:HIS44 4.8 4.6 1.0
O O:HIS44 4.8 3.3 1.0
O O:HOH803 4.9 19.6 1.0

Copper binding site 2 out of 4 in 1sda

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Copper binding site 2 out of 4 in the Crystal Structure of Peroxynitrite-Modified Bovine Cu,Zn Superoxide Dismutase


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 Peroxynitrite-Modified Bovine Cu,Zn Superoxide Dismutase within 5.0Å range:
probe atom residue distance (Å) B Occ
Y:Cu804

b:20.2
occ:1.00
ND1 Y:HIS44 1.8 9.7 1.0
NE2 Y:HIS118 2.0 9.8 1.0
NE2 Y:HIS61 2.1 6.6 1.0
NE2 Y:HIS46 2.3 6.3 1.0
CG Y:HIS44 2.7 8.8 1.0
CD2 Y:HIS61 2.8 4.2 1.0
CE1 Y:HIS118 2.8 10.0 1.0
CE1 Y:HIS44 2.9 9.9 1.0
CD2 Y:HIS118 3.0 9.6 1.0
CB Y:HIS44 3.0 7.5 1.0
CE1 Y:HIS46 3.1 3.8 1.0
CE1 Y:HIS61 3.2 6.4 1.0
CD2 Y:HIS46 3.3 3.6 1.0
CD2 Y:HIS44 3.9 8.9 1.0
NE2 Y:HIS44 3.9 9.3 1.0
ND1 Y:HIS118 4.0 9.9 1.0
CG Y:HIS61 4.0 4.9 1.0
CG Y:HIS118 4.1 10.9 1.0
ND1 Y:HIS61 4.2 8.8 1.0
ND1 Y:HIS46 4.3 4.2 1.0
CA Y:HIS44 4.4 6.9 1.0
CG Y:HIS46 4.4 3.5 1.0
N Y:HIS44 4.6 7.6 1.0
O Y:HOH806 4.7 17.8 1.0
CG1 Y:VAL116 4.9 8.9 1.0
O Y:THR135 4.9 14.7 1.0
O Y:HIS44 5.0 9.2 1.0
C Y:HIS44 5.0 7.4 1.0
CB Y:VAL116 5.0 8.7 1.0

Copper binding site 3 out of 4 in 1sda

Go back to Copper Binding Sites List in 1sda
Copper binding site 3 out of 4 in the Crystal Structure of Peroxynitrite-Modified Bovine Cu,Zn Superoxide Dismutase


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 Peroxynitrite-Modified Bovine Cu,Zn Superoxide Dismutase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu807

b:13.4
occ:1.00
ND1 B:HIS44 1.9 7.4 1.0
NE2 B:HIS118 2.0 9.5 1.0
NE2 B:HIS46 2.1 5.9 1.0
NE2 B:HIS61 2.3 9.8 1.0
CG B:HIS44 2.8 8.2 1.0
CE1 B:HIS46 2.8 6.7 1.0
CD2 B:HIS61 2.8 8.6 1.0
CE1 B:HIS118 2.9 9.0 1.0
CD2 B:HIS118 3.0 9.8 1.0
CE1 B:HIS44 3.0 9.8 1.0
CB B:HIS44 3.1 7.6 1.0
CD2 B:HIS46 3.2 5.2 1.0
CE1 B:HIS61 3.4 9.9 1.0
CD2 B:HIS44 3.9 7.9 1.0
ND1 B:HIS46 4.0 7.4 1.0
NE2 B:HIS44 4.0 7.2 1.0
ND1 B:HIS118 4.1 10.6 1.0
CG B:HIS118 4.1 10.1 1.0
CG B:HIS61 4.1 8.1 1.0
CG B:HIS46 4.2 6.1 1.0
ND1 B:HIS61 4.4 9.1 1.0
CA B:HIS44 4.5 4.8 1.0
O B:HOH809 4.6 12.5 1.0
CG1 B:VAL116 4.6 5.0 1.0
N B:HIS44 4.8 6.6 1.0
CB B:VAL116 4.8 6.1 1.0

Copper binding site 4 out of 4 in 1sda

Go back to Copper Binding Sites List in 1sda
Copper binding site 4 out of 4 in the Crystal Structure of Peroxynitrite-Modified Bovine Cu,Zn Superoxide Dismutase


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 Peroxynitrite-Modified Bovine Cu,Zn Superoxide Dismutase within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Cu810

b:21.7
occ:1.00
ND1 G:HIS44 1.8 11.7 1.0
NE2 G:HIS46 2.1 7.1 1.0
NE2 G:HIS118 2.1 9.4 1.0
NE2 G:HIS61 2.2 14.2 1.0
CD2 G:HIS61 2.7 13.3 1.0
CE1 G:HIS44 2.7 10.1 1.0
CG G:HIS44 2.8 10.0 1.0
CE1 G:HIS118 2.9 9.1 1.0
CE1 G:HIS46 3.0 6.3 1.0
CD2 G:HIS46 3.1 5.5 1.0
CB G:HIS44 3.2 8.9 1.0
CD2 G:HIS118 3.2 9.6 1.0
CE1 G:HIS61 3.4 14.5 1.0
NE2 G:HIS44 3.8 10.1 1.0
CD2 G:HIS44 3.8 8.7 1.0
CG G:HIS61 3.9 11.8 1.0
ND1 G:HIS118 4.1 6.8 1.0
ND1 G:HIS46 4.2 6.4 1.0
CG G:HIS46 4.2 5.5 1.0
ND1 G:HIS61 4.2 14.4 1.0
CG G:HIS118 4.3 10.0 1.0
CA G:HIS44 4.4 10.0 1.0
N G:HIS44 4.6 10.3 1.0
CB G:VAL116 4.7 4.1 1.0
CG1 G:VAL116 4.9 2.8 1.0
C G:HIS44 5.0 9.5 1.0

Reference:

C.D.Smith, M.Carson, M.Van Der Woerd, J.Chen, H.Ischiropoulos, J.S.Beckman. Crystal Structure of Peroxynitrite-Modified Bovine Cu,Zn Superoxide Dismutase. Arch.Biochem.Biophys. V. 299 350 1992.
ISSN: ISSN 0003-9861
PubMed: 1444476
DOI: 10.1016/0003-9861(92)90286-6
Page generated: Sun Dec 13 11:01:51 2020

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