Zinc in PDB 1l3n: The Solution Structure of Reduced Dimeric Copper Zinc Sod: the Structural Effects of Dimerization
Enzymatic activity of The Solution Structure of Reduced Dimeric Copper Zinc Sod: the Structural Effects of Dimerization
All present enzymatic activity of The Solution Structure of Reduced Dimeric Copper Zinc Sod: the Structural Effects of Dimerization:
1.15.1.1;
Other elements in 1l3n:
The structure of The Solution Structure of Reduced Dimeric Copper Zinc Sod: the Structural Effects of Dimerization also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the The Solution Structure of Reduced Dimeric Copper Zinc Sod: the Structural Effects of Dimerization
(pdb code 1l3n). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the
The Solution Structure of Reduced Dimeric Copper Zinc Sod: the Structural Effects of Dimerization, PDB code: 1l3n:
Jump to Zinc binding site number:
1;
2;
Zinc binding site 1 out
of 2 in 1l3n
Go back to
Zinc Binding Sites List in 1l3n
Zinc binding site 1 out
of 2 in the The Solution Structure of Reduced Dimeric Copper Zinc Sod: the Structural Effects of Dimerization
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of The Solution Structure of Reduced Dimeric Copper Zinc Sod: the Structural Effects of Dimerization within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn155
b:10.0
occ:1.00
|
OD1
|
A:ASP83
|
1.8
|
10.0
|
1.0
|
ND1
|
A:HIS71
|
2.1
|
10.0
|
1.0
|
ND1
|
A:HIS63
|
2.1
|
10.0
|
1.0
|
ND1
|
A:HIS80
|
2.1
|
10.0
|
1.0
|
CG
|
A:ASP83
|
2.5
|
10.0
|
1.0
|
OD2
|
A:ASP83
|
2.6
|
10.0
|
1.0
|
CE1
|
A:HIS71
|
2.9
|
10.0
|
1.0
|
CE1
|
A:HIS80
|
3.0
|
10.0
|
1.0
|
HA
|
A:HIS71
|
3.0
|
10.0
|
1.0
|
CE1
|
A:HIS63
|
3.0
|
10.0
|
1.0
|
HE1
|
A:HIS71
|
3.1
|
10.0
|
1.0
|
O
|
A:LYS136
|
3.1
|
10.0
|
1.0
|
HB2
|
A:HIS80
|
3.1
|
10.0
|
1.0
|
CG
|
A:HIS63
|
3.1
|
10.0
|
1.0
|
HE1
|
A:HIS80
|
3.1
|
10.0
|
1.0
|
CG
|
A:HIS80
|
3.2
|
10.0
|
1.0
|
CG
|
A:HIS71
|
3.2
|
10.0
|
1.0
|
HE1
|
A:HIS63
|
3.3
|
10.0
|
1.0
|
HB3
|
A:HIS63
|
3.3
|
10.0
|
1.0
|
HB2
|
A:HIS63
|
3.5
|
10.0
|
1.0
|
CB
|
A:HIS63
|
3.6
|
10.0
|
1.0
|
CB
|
A:HIS80
|
3.7
|
10.0
|
1.0
|
HB2
|
A:HIS71
|
3.7
|
10.0
|
1.0
|
CB
|
A:HIS71
|
3.8
|
10.0
|
1.0
|
CA
|
A:HIS71
|
3.8
|
10.0
|
1.0
|
CB
|
A:ASP83
|
3.9
|
10.0
|
1.0
|
H
|
A:HIS80
|
3.9
|
10.0
|
1.0
|
HA
|
A:THR137
|
3.9
|
10.0
|
1.0
|
H
|
A:GLY72
|
4.0
|
10.0
|
1.0
|
NE2
|
A:HIS71
|
4.1
|
10.0
|
1.0
|
NE2
|
A:HIS80
|
4.1
|
10.0
|
1.0
|
HB3
|
A:ASP83
|
4.1
|
10.0
|
1.0
|
NE2
|
A:HIS63
|
4.2
|
10.0
|
1.0
|
HB3
|
A:HIS46
|
4.2
|
10.0
|
1.0
|
CD2
|
A:HIS63
|
4.2
|
10.0
|
1.0
|
CD2
|
A:HIS80
|
4.2
|
10.0
|
1.0
|
CD2
|
A:HIS71
|
4.3
|
10.0
|
1.0
|
HB3
|
A:HIS80
|
4.3
|
10.0
|
1.0
|
C
|
A:LYS136
|
4.3
|
10.0
|
1.0
|
HA
|
A:ASP83
|
4.4
|
10.0
|
1.0
|
HB2
|
A:ASP83
|
4.6
|
10.0
|
1.0
|
N
|
A:GLY72
|
4.7
|
10.0
|
1.0
|
CA
|
A:ASP83
|
4.7
|
10.0
|
1.0
|
N
|
A:HIS80
|
4.7
|
10.0
|
1.0
|
HD2
|
A:HIS46
|
4.7
|
10.0
|
1.0
|
C
|
A:HIS71
|
4.8
|
10.0
|
1.0
|
HB3
|
A:HIS71
|
4.8
|
10.0
|
1.0
|
CA
|
A:HIS80
|
4.8
|
10.0
|
1.0
|
N
|
A:HIS71
|
4.9
|
10.0
|
1.0
|
HA
|
A:LYS136
|
4.9
|
10.0
|
1.0
|
CA
|
A:THR137
|
4.9
|
10.0
|
1.0
|
CD2
|
A:HIS46
|
4.9
|
10.0
|
1.0
|
HE2
|
A:HIS80
|
5.0
|
10.0
|
1.0
|
HE2
|
A:HIS71
|
5.0
|
10.0
|
1.0
|
|
Zinc binding site 2 out
of 2 in 1l3n
Go back to
Zinc Binding Sites List in 1l3n
Zinc binding site 2 out
of 2 in the The Solution Structure of Reduced Dimeric Copper Zinc Sod: the Structural Effects of Dimerization
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of The Solution Structure of Reduced Dimeric Copper Zinc Sod: the Structural Effects of Dimerization within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn155
b:10.0
occ:1.00
|
OD1
|
B:ASP83
|
1.9
|
10.0
|
1.0
|
ND1
|
B:HIS80
|
2.0
|
10.0
|
1.0
|
ND1
|
B:HIS71
|
2.0
|
10.0
|
1.0
|
ND1
|
B:HIS63
|
2.1
|
10.0
|
1.0
|
CG
|
B:ASP83
|
2.5
|
10.0
|
1.0
|
OD2
|
B:ASP83
|
2.6
|
10.0
|
1.0
|
HA
|
B:HIS71
|
2.9
|
10.0
|
1.0
|
CE1
|
B:HIS71
|
3.0
|
10.0
|
1.0
|
CE1
|
B:HIS80
|
3.0
|
10.0
|
1.0
|
CE1
|
B:HIS63
|
3.0
|
10.0
|
1.0
|
HB2
|
B:HIS80
|
3.0
|
10.0
|
1.0
|
CG
|
B:HIS80
|
3.1
|
10.0
|
1.0
|
HE1
|
B:HIS71
|
3.1
|
10.0
|
1.0
|
CG
|
B:HIS63
|
3.1
|
10.0
|
1.0
|
HE1
|
B:HIS80
|
3.2
|
10.0
|
1.0
|
CG
|
B:HIS71
|
3.2
|
10.0
|
1.0
|
HE1
|
B:HIS63
|
3.3
|
10.0
|
1.0
|
HB3
|
B:HIS63
|
3.4
|
10.0
|
1.0
|
CB
|
B:HIS80
|
3.6
|
10.0
|
1.0
|
HB2
|
B:HIS71
|
3.6
|
10.0
|
1.0
|
CB
|
B:HIS63
|
3.7
|
10.0
|
1.0
|
CB
|
B:HIS71
|
3.7
|
10.0
|
1.0
|
HB2
|
B:HIS63
|
3.7
|
10.0
|
1.0
|
CA
|
B:HIS71
|
3.8
|
10.0
|
1.0
|
HA
|
B:THR137
|
3.8
|
10.0
|
1.0
|
H
|
B:HIS80
|
3.9
|
10.0
|
1.0
|
H
|
B:GLY72
|
3.9
|
10.0
|
1.0
|
CB
|
B:ASP83
|
3.9
|
10.0
|
1.0
|
O
|
B:LYS136
|
4.0
|
10.0
|
1.0
|
NE2
|
B:HIS80
|
4.1
|
10.0
|
1.0
|
NE2
|
B:HIS71
|
4.1
|
10.0
|
1.0
|
HB3
|
B:ASP83
|
4.2
|
10.0
|
1.0
|
CD2
|
B:HIS80
|
4.2
|
10.0
|
1.0
|
NE2
|
B:HIS63
|
4.2
|
10.0
|
1.0
|
HB3
|
B:HIS80
|
4.2
|
10.0
|
1.0
|
CD2
|
B:HIS63
|
4.2
|
10.0
|
1.0
|
CD2
|
B:HIS71
|
4.2
|
10.0
|
1.0
|
HA
|
B:ASP83
|
4.4
|
10.0
|
1.0
|
HB3
|
B:HIS46
|
4.5
|
10.0
|
1.0
|
N
|
B:GLY72
|
4.7
|
10.0
|
1.0
|
HB2
|
B:ASP83
|
4.7
|
10.0
|
1.0
|
N
|
B:HIS80
|
4.7
|
10.0
|
1.0
|
C
|
B:HIS71
|
4.7
|
10.0
|
1.0
|
CA
|
B:ASP83
|
4.7
|
10.0
|
1.0
|
HB3
|
B:HIS71
|
4.8
|
10.0
|
1.0
|
N
|
B:HIS71
|
4.8
|
10.0
|
1.0
|
CA
|
B:HIS80
|
4.8
|
10.0
|
1.0
|
C
|
B:LYS136
|
4.8
|
10.0
|
1.0
|
CA
|
B:THR137
|
4.9
|
10.0
|
1.0
|
H
|
B:VAL81
|
4.9
|
10.0
|
1.0
|
HE2
|
B:HIS80
|
5.0
|
10.0
|
1.0
|
HD2
|
B:HIS46
|
5.0
|
10.0
|
1.0
|
|
Reference:
L.Banci,
I.Bertini,
F.Cramaro,
R.Del Conte,
M.S.Viezzoli.
The Solution Structure of Reduced Dimeric Copper Zinc Superoxide Dismutase. the Structural Effects of Dimerization Eur.J.Biochem. V. 269 1905 2002.
ISSN: ISSN 0014-2956
PubMed: 11952792
DOI: 10.1046/J.1432-1033.2002.02840.X
Page generated: Sun Oct 13 04:49:01 2024
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