Zinc in PDB 1s7g: Structural Basis For the Mechanism and Regulation of SIR2 Enzymes
Protein crystallography data
The structure of Structural Basis For the Mechanism and Regulation of SIR2 Enzymes, PDB code: 1s7g
was solved by
J.L.Avalos,
J.D.Boeke,
C.Wolberger,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
29.78 /
2.30
|
Space group
|
P 21 21 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
104.850,
181.574,
78.921,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
20.7 /
24.9
|
Zinc Binding Sites:
The binding sites of Zinc atom in the Structural Basis For the Mechanism and Regulation of SIR2 Enzymes
(pdb code 1s7g). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 9 binding sites of Zinc where determined in the
Structural Basis For the Mechanism and Regulation of SIR2 Enzymes, PDB code: 1s7g:
Jump to Zinc binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
Zinc binding site 1 out
of 9 in 1s7g
Go back to
Zinc Binding Sites List in 1s7g
Zinc binding site 1 out
of 9 in the Structural Basis For the Mechanism and Regulation of SIR2 Enzymes
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Structural Basis For the Mechanism and Regulation of SIR2 Enzymes within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn601
b:32.7
occ:1.00
|
SG
|
A:CYS129
|
2.4
|
28.7
|
1.0
|
SG
|
A:CYS126
|
2.4
|
27.9
|
1.0
|
SG
|
A:CYS153
|
2.4
|
34.4
|
1.0
|
SG
|
A:CYS150
|
2.4
|
32.9
|
1.0
|
CB
|
A:CYS129
|
3.2
|
29.8
|
1.0
|
CB
|
A:CYS126
|
3.2
|
26.0
|
1.0
|
CB
|
A:CYS150
|
3.3
|
32.4
|
1.0
|
CB
|
A:CYS153
|
3.3
|
34.0
|
1.0
|
N
|
A:CYS129
|
3.6
|
31.2
|
1.0
|
CA
|
A:CYS129
|
3.9
|
30.1
|
1.0
|
N
|
A:CYS153
|
3.9
|
36.0
|
1.0
|
CA
|
A:CYS153
|
4.2
|
35.1
|
1.0
|
CB
|
A:SER155
|
4.4
|
30.5
|
1.0
|
C
|
A:CYS129
|
4.6
|
30.5
|
1.0
|
CA
|
A:CYS126
|
4.7
|
28.1
|
1.0
|
CB
|
A:GLU131
|
4.7
|
36.4
|
1.0
|
N
|
A:HIS130
|
4.7
|
30.5
|
1.0
|
C
|
A:ASP128
|
4.7
|
32.4
|
1.0
|
CA
|
A:CYS150
|
4.7
|
34.4
|
1.0
|
C
|
A:CYS153
|
4.8
|
35.6
|
1.0
|
CB
|
A:ASP128
|
4.8
|
35.0
|
1.0
|
N
|
A:SER155
|
4.9
|
33.0
|
1.0
|
N
|
A:GLU131
|
4.9
|
32.9
|
1.0
|
N
|
A:GLY154
|
4.9
|
34.6
|
1.0
|
C
|
A:LYS152
|
4.9
|
38.0
|
1.0
|
|
Zinc binding site 2 out
of 9 in 1s7g
Go back to
Zinc Binding Sites List in 1s7g
Zinc binding site 2 out
of 9 in the Structural Basis For the Mechanism and Regulation of SIR2 Enzymes
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Structural Basis For the Mechanism and Regulation of SIR2 Enzymes within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn602
b:32.4
occ:1.00
|
NE2
|
A:HIS17
|
2.1
|
35.7
|
1.0
|
NE2
|
C:HIS130
|
2.1
|
27.5
|
1.0
|
NE2
|
A:HIS183
|
2.2
|
30.0
|
1.0
|
OE1
|
A:GLU180
|
2.4
|
38.5
|
1.0
|
OE2
|
A:GLU180
|
2.4
|
34.6
|
1.0
|
CD
|
A:GLU180
|
2.7
|
35.5
|
1.0
|
CE1
|
A:HIS17
|
3.0
|
38.3
|
1.0
|
CE1
|
C:HIS130
|
3.1
|
27.9
|
1.0
|
CD2
|
C:HIS130
|
3.1
|
25.5
|
1.0
|
CE1
|
A:HIS183
|
3.1
|
33.1
|
1.0
|
CD2
|
A:HIS17
|
3.2
|
38.2
|
1.0
|
CD2
|
A:HIS183
|
3.2
|
29.5
|
1.0
|
ND1
|
A:HIS17
|
4.2
|
36.4
|
1.0
|
ND1
|
C:HIS130
|
4.2
|
27.1
|
1.0
|
CG
|
A:GLU180
|
4.2
|
31.4
|
1.0
|
CG
|
C:HIS130
|
4.2
|
28.7
|
1.0
|
CG
|
A:HIS17
|
4.3
|
36.3
|
1.0
|
ND1
|
A:HIS183
|
4.3
|
31.9
|
1.0
|
CG
|
A:HIS183
|
4.4
|
31.6
|
1.0
|
CB
|
A:LYS95
|
4.7
|
27.5
|
1.0
|
CA
|
A:GLU180
|
4.7
|
24.1
|
1.0
|
O
|
A:HOH711
|
4.7
|
34.4
|
1.0
|
O
|
C:ASP128
|
4.8
|
34.1
|
1.0
|
CB
|
A:GLU180
|
4.8
|
25.9
|
1.0
|
|
Zinc binding site 3 out
of 9 in 1s7g
Go back to
Zinc Binding Sites List in 1s7g
Zinc binding site 3 out
of 9 in the Structural Basis For the Mechanism and Regulation of SIR2 Enzymes
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Structural Basis For the Mechanism and Regulation of SIR2 Enzymes within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn603
b:32.4
occ:1.00
|
SG
|
B:CYS129
|
2.3
|
34.3
|
1.0
|
SG
|
B:CYS150
|
2.4
|
31.3
|
1.0
|
SG
|
B:CYS126
|
2.4
|
33.5
|
1.0
|
SG
|
B:CYS153
|
2.4
|
39.3
|
1.0
|
CB
|
B:CYS150
|
3.1
|
32.7
|
1.0
|
CB
|
B:CYS126
|
3.2
|
27.4
|
1.0
|
CB
|
B:CYS129
|
3.2
|
31.8
|
1.0
|
CB
|
B:CYS153
|
3.4
|
39.8
|
1.0
|
N
|
B:CYS129
|
3.7
|
34.9
|
1.0
|
N
|
B:CYS153
|
3.8
|
41.5
|
1.0
|
CA
|
B:CYS129
|
4.0
|
33.3
|
1.0
|
CA
|
B:CYS153
|
4.1
|
40.8
|
1.0
|
CA
|
B:CYS150
|
4.6
|
34.8
|
1.0
|
C
|
B:CYS129
|
4.6
|
32.0
|
1.0
|
CA
|
B:CYS126
|
4.6
|
25.4
|
1.0
|
CB
|
B:SER155
|
4.7
|
37.2
|
1.0
|
CB
|
B:ASP128
|
4.7
|
40.0
|
1.0
|
CB
|
B:GLU131
|
4.7
|
31.4
|
1.0
|
N
|
B:HIS130
|
4.7
|
30.6
|
1.0
|
CB
|
B:LYS152
|
4.7
|
42.1
|
1.0
|
C
|
B:LYS152
|
4.8
|
41.7
|
1.0
|
C
|
B:CYS153
|
4.8
|
40.1
|
1.0
|
C
|
B:ASP128
|
4.8
|
35.3
|
1.0
|
N
|
B:GLU131
|
4.9
|
29.8
|
1.0
|
N
|
B:GLY154
|
4.9
|
40.0
|
1.0
|
N
|
B:SER155
|
4.9
|
36.5
|
1.0
|
|
Zinc binding site 4 out
of 9 in 1s7g
Go back to
Zinc Binding Sites List in 1s7g
Zinc binding site 4 out
of 9 in the Structural Basis For the Mechanism and Regulation of SIR2 Enzymes
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of Structural Basis For the Mechanism and Regulation of SIR2 Enzymes within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn604
b:28.9
occ:1.00
|
OE1
|
B:GLU180
|
2.1
|
27.4
|
1.0
|
NE2
|
B:HIS183
|
2.1
|
29.7
|
1.0
|
NE2
|
B:HIS17
|
2.2
|
28.0
|
1.0
|
CD
|
B:GLU180
|
2.9
|
29.9
|
1.0
|
CE1
|
B:HIS183
|
2.9
|
32.2
|
1.0
|
OE2
|
B:GLU180
|
3.1
|
31.5
|
1.0
|
CD2
|
B:HIS17
|
3.1
|
29.6
|
1.0
|
CD2
|
B:HIS183
|
3.2
|
29.1
|
1.0
|
CE1
|
B:HIS17
|
3.3
|
27.7
|
1.0
|
ND1
|
B:HIS183
|
4.1
|
31.7
|
1.0
|
CG
|
B:HIS183
|
4.2
|
30.8
|
1.0
|
CG
|
B:HIS17
|
4.3
|
29.3
|
1.0
|
CG
|
B:GLU180
|
4.3
|
27.4
|
1.0
|
ND1
|
B:HIS17
|
4.4
|
29.0
|
1.0
|
CA
|
B:GLU180
|
4.7
|
29.1
|
1.0
|
O
|
B:GLU180
|
4.8
|
30.1
|
1.0
|
CB
|
B:LYS95
|
5.0
|
25.5
|
1.0
|
NE
|
B:ARG113
|
5.0
|
32.0
|
1.0
|
CB
|
B:GLU180
|
5.0
|
29.9
|
1.0
|
|
Zinc binding site 5 out
of 9 in 1s7g
Go back to
Zinc Binding Sites List in 1s7g
Zinc binding site 5 out
of 9 in the Structural Basis For the Mechanism and Regulation of SIR2 Enzymes
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 5 of Structural Basis For the Mechanism and Regulation of SIR2 Enzymes within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn605
b:32.2
occ:1.00
|
SG
|
C:CYS126
|
2.4
|
28.9
|
1.0
|
SG
|
C:CYS153
|
2.4
|
35.6
|
1.0
|
SG
|
C:CYS150
|
2.4
|
32.2
|
1.0
|
SG
|
C:CYS129
|
2.4
|
30.7
|
1.0
|
CB
|
C:CYS126
|
3.2
|
25.4
|
1.0
|
CB
|
C:CYS150
|
3.2
|
32.7
|
1.0
|
CB
|
C:CYS129
|
3.2
|
29.6
|
1.0
|
CB
|
C:CYS153
|
3.5
|
38.5
|
1.0
|
N
|
C:CYS129
|
3.7
|
31.4
|
1.0
|
N
|
C:CYS153
|
3.9
|
41.6
|
1.0
|
CA
|
C:CYS129
|
4.0
|
30.6
|
1.0
|
CA
|
C:CYS153
|
4.2
|
39.9
|
1.0
|
CB
|
C:SER155
|
4.4
|
33.8
|
1.0
|
C
|
C:CYS129
|
4.6
|
28.9
|
1.0
|
CA
|
C:CYS126
|
4.6
|
27.2
|
1.0
|
CA
|
C:CYS150
|
4.6
|
34.9
|
1.0
|
CB
|
C:GLU131
|
4.7
|
32.9
|
1.0
|
CB
|
C:LYS152
|
4.7
|
44.0
|
1.0
|
N
|
C:HIS130
|
4.7
|
30.4
|
1.0
|
N
|
C:GLU131
|
4.8
|
29.8
|
1.0
|
CB
|
C:ASP128
|
4.8
|
37.8
|
1.0
|
C
|
C:ASP128
|
4.8
|
32.9
|
1.0
|
C
|
C:LYS152
|
4.8
|
42.7
|
1.0
|
C
|
C:CYS153
|
4.9
|
38.8
|
1.0
|
N
|
C:SER155
|
4.9
|
34.5
|
1.0
|
N
|
C:GLY154
|
5.0
|
38.2
|
1.0
|
|
Zinc binding site 6 out
of 9 in 1s7g
Go back to
Zinc Binding Sites List in 1s7g
Zinc binding site 6 out
of 9 in the Structural Basis For the Mechanism and Regulation of SIR2 Enzymes
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 6 of Structural Basis For the Mechanism and Regulation of SIR2 Enzymes within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn606
b:33.2
occ:1.00
|
NE2
|
A:HIS130
|
2.1
|
29.7
|
1.0
|
NE2
|
C:HIS17
|
2.2
|
38.8
|
1.0
|
NE2
|
C:HIS183
|
2.2
|
43.2
|
1.0
|
OE2
|
C:GLU180
|
2.4
|
47.9
|
1.0
|
OE1
|
C:GLU180
|
2.6
|
49.4
|
1.0
|
CD
|
C:GLU180
|
2.8
|
47.2
|
1.0
|
CE1
|
A:HIS130
|
2.9
|
28.1
|
1.0
|
CD2
|
C:HIS17
|
3.1
|
39.5
|
1.0
|
CE1
|
C:HIS183
|
3.1
|
41.7
|
1.0
|
CD2
|
A:HIS130
|
3.2
|
27.5
|
1.0
|
CD2
|
C:HIS183
|
3.3
|
41.9
|
1.0
|
CE1
|
C:HIS17
|
3.3
|
40.9
|
1.0
|
ND1
|
A:HIS130
|
4.1
|
28.2
|
1.0
|
CG
|
C:GLU180
|
4.2
|
41.5
|
1.0
|
ND1
|
C:HIS183
|
4.3
|
42.2
|
1.0
|
CG
|
A:HIS130
|
4.3
|
28.0
|
1.0
|
CG
|
C:HIS17
|
4.3
|
38.7
|
1.0
|
CG
|
C:HIS183
|
4.4
|
41.7
|
1.0
|
ND1
|
C:HIS17
|
4.4
|
39.5
|
1.0
|
CA
|
C:GLU180
|
4.6
|
33.1
|
1.0
|
O
|
A:ASP128
|
4.6
|
35.6
|
1.0
|
CB
|
C:GLU180
|
4.8
|
37.2
|
1.0
|
CB
|
C:ALA96
|
4.9
|
33.1
|
1.0
|
|
Zinc binding site 7 out
of 9 in 1s7g
Go back to
Zinc Binding Sites List in 1s7g
Zinc binding site 7 out
of 9 in the Structural Basis For the Mechanism and Regulation of SIR2 Enzymes
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 7 of Structural Basis For the Mechanism and Regulation of SIR2 Enzymes within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Zn607
b:27.3
occ:1.00
|
SG
|
D:CYS126
|
2.3
|
24.6
|
1.0
|
SG
|
D:CYS129
|
2.3
|
24.7
|
1.0
|
SG
|
D:CYS150
|
2.4
|
26.5
|
1.0
|
SG
|
D:CYS153
|
2.4
|
26.5
|
1.0
|
CB
|
D:CYS126
|
3.2
|
19.9
|
1.0
|
CB
|
D:CYS150
|
3.2
|
25.6
|
1.0
|
CB
|
D:CYS129
|
3.3
|
22.4
|
1.0
|
CB
|
D:CYS153
|
3.3
|
28.6
|
1.0
|
N
|
D:CYS129
|
3.7
|
24.8
|
1.0
|
N
|
D:CYS153
|
3.8
|
32.2
|
1.0
|
CA
|
D:CYS129
|
4.0
|
24.6
|
1.0
|
CA
|
D:CYS153
|
4.1
|
29.7
|
1.0
|
CB
|
D:SER155
|
4.4
|
23.0
|
1.0
|
C
|
D:CYS129
|
4.6
|
23.4
|
1.0
|
CA
|
D:CYS126
|
4.6
|
20.5
|
1.0
|
CA
|
D:CYS150
|
4.7
|
25.9
|
1.0
|
C
|
D:CYS153
|
4.7
|
28.6
|
1.0
|
N
|
D:HIS130
|
4.7
|
23.1
|
1.0
|
CB
|
D:LYS152
|
4.8
|
32.2
|
1.0
|
C
|
D:ASP128
|
4.8
|
25.5
|
1.0
|
CB
|
D:GLU131
|
4.8
|
28.7
|
1.0
|
C
|
D:LYS152
|
4.8
|
33.3
|
1.0
|
N
|
D:GLY154
|
4.8
|
29.0
|
1.0
|
N
|
D:SER155
|
4.8
|
23.7
|
1.0
|
CB
|
D:ASP128
|
4.8
|
28.9
|
1.0
|
N
|
D:GLU131
|
4.9
|
25.9
|
1.0
|
|
Zinc binding site 8 out
of 9 in 1s7g
Go back to
Zinc Binding Sites List in 1s7g
Zinc binding site 8 out
of 9 in the Structural Basis For the Mechanism and Regulation of SIR2 Enzymes
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 8 of Structural Basis For the Mechanism and Regulation of SIR2 Enzymes within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Zn608
b:31.9
occ:1.00
|
NE2
|
D:HIS183
|
2.1
|
41.7
|
1.0
|
NE2
|
D:HIS17
|
2.2
|
35.2
|
1.0
|
OE2
|
D:GLU180
|
2.2
|
37.5
|
1.0
|
CD
|
D:GLU180
|
2.9
|
40.1
|
1.0
|
CE1
|
D:HIS183
|
3.0
|
42.9
|
1.0
|
OE1
|
D:GLU180
|
3.1
|
39.9
|
1.0
|
CE1
|
D:HIS17
|
3.1
|
36.1
|
1.0
|
CD2
|
D:HIS183
|
3.2
|
39.1
|
1.0
|
CD2
|
D:HIS17
|
3.2
|
34.1
|
1.0
|
ND1
|
D:HIS183
|
4.1
|
43.4
|
1.0
|
ND1
|
D:HIS17
|
4.2
|
35.7
|
1.0
|
CG
|
D:GLU180
|
4.3
|
35.4
|
1.0
|
CG
|
D:HIS183
|
4.3
|
39.0
|
1.0
|
CG
|
D:HIS17
|
4.3
|
36.3
|
1.0
|
CA
|
D:GLU180
|
4.4
|
29.3
|
1.0
|
CB
|
D:GLU180
|
4.7
|
32.0
|
1.0
|
CB
|
D:LYS95
|
4.8
|
31.7
|
1.0
|
O
|
D:HOH623
|
4.9
|
36.6
|
1.0
|
|
Zinc binding site 9 out
of 9 in 1s7g
Go back to
Zinc Binding Sites List in 1s7g
Zinc binding site 9 out
of 9 in the Structural Basis For the Mechanism and Regulation of SIR2 Enzymes
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 9 of Structural Basis For the Mechanism and Regulation of SIR2 Enzymes within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Zn609
b:31.9
occ:1.00
|
SG
|
E:CYS129
|
2.2
|
34.3
|
1.0
|
SG
|
E:CYS126
|
2.4
|
34.0
|
1.0
|
SG
|
E:CYS153
|
2.4
|
31.3
|
1.0
|
SG
|
E:CYS150
|
2.4
|
33.0
|
1.0
|
CB
|
E:CYS150
|
3.1
|
33.0
|
1.0
|
CB
|
E:CYS153
|
3.2
|
31.1
|
1.0
|
CB
|
E:CYS129
|
3.2
|
35.8
|
1.0
|
CB
|
E:CYS126
|
3.2
|
29.6
|
1.0
|
N
|
E:CYS129
|
3.6
|
34.6
|
1.0
|
N
|
E:CYS153
|
3.7
|
32.3
|
1.0
|
CA
|
E:CYS129
|
4.0
|
35.6
|
1.0
|
CA
|
E:CYS153
|
4.0
|
30.6
|
1.0
|
CB
|
E:SER155
|
4.3
|
34.8
|
1.0
|
CB
|
E:ASP128
|
4.5
|
38.0
|
1.0
|
CA
|
E:CYS150
|
4.6
|
36.0
|
1.0
|
C
|
E:CYS153
|
4.6
|
30.1
|
1.0
|
C
|
E:ASP128
|
4.7
|
34.9
|
1.0
|
CA
|
E:CYS126
|
4.7
|
32.2
|
1.0
|
C
|
E:CYS129
|
4.7
|
36.6
|
1.0
|
CB
|
E:LYS152
|
4.7
|
36.8
|
1.0
|
N
|
E:SER155
|
4.7
|
34.0
|
1.0
|
C
|
E:LYS152
|
4.8
|
34.0
|
1.0
|
CB
|
E:GLU131
|
4.8
|
43.6
|
1.0
|
N
|
E:GLY154
|
4.8
|
31.8
|
1.0
|
N
|
E:HIS130
|
4.9
|
38.4
|
1.0
|
CA
|
E:ASP128
|
5.0
|
35.7
|
1.0
|
|
Reference:
J.L.Avalos,
J.D.Boeke,
C.Wolberger.
Structural Basis For the Mechanism and Regulation of SIR2 Enzymes Mol.Cell V. 13 639 2004.
ISSN: ISSN 1097-2765
PubMed: 15023335
DOI: 10.1016/S1097-2765(04)00082-6
Page generated: Wed Oct 16 18:46:38 2024
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