Zinc in PDB 1b0n: Sinr Protein/Sini Protein Complex
Protein crystallography data
The structure of Sinr Protein/Sini Protein Complex, PDB code: 1b0n
was solved by
R.J.Lewis,
J.A.Brannigan,
W.A.Offen,
I.Smith,
A.J.Wilkinson,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
20.00 /
1.90
|
Space group
|
P 31 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
60.900,
60.900,
87.740,
90.00,
90.00,
120.00
|
R / Rfree (%)
|
19.9 /
24.5
|
Zinc Binding Sites:
The binding sites of Zinc atom in the Sinr Protein/Sini Protein Complex
(pdb code 1b0n). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 5 binding sites of Zinc where determined in the
Sinr Protein/Sini Protein Complex, PDB code: 1b0n:
Jump to Zinc binding site number:
1;
2;
3;
4;
5;
Zinc binding site 1 out
of 5 in 1b0n
Go back to
Zinc Binding Sites List in 1b0n
Zinc binding site 1 out
of 5 in the Sinr Protein/Sini Protein Complex
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Sinr Protein/Sini Protein Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn1001
b:30.4
occ:1.00
|
OD2
|
A:ASP63
|
1.8
|
34.6
|
1.0
|
NE2
|
A:HIS66
|
1.8
|
30.3
|
1.0
|
OE2
|
B:GLU17
|
2.0
|
33.5
|
1.0
|
OE2
|
B:GLU21
|
2.1
|
31.2
|
1.0
|
OE1
|
B:GLU17
|
2.6
|
29.2
|
1.0
|
CD
|
B:GLU17
|
2.7
|
28.3
|
1.0
|
CG
|
A:ASP63
|
2.8
|
30.0
|
1.0
|
CD2
|
A:HIS66
|
2.8
|
31.3
|
1.0
|
CE1
|
A:HIS66
|
2.9
|
32.9
|
1.0
|
CD
|
B:GLU21
|
3.0
|
32.6
|
1.0
|
OD1
|
A:ASP63
|
3.4
|
29.6
|
1.0
|
CG
|
B:GLU21
|
3.4
|
25.9
|
1.0
|
NZ
|
A:LYS65
|
3.5
|
39.4
|
1.0
|
ND1
|
A:HIS66
|
4.0
|
31.6
|
1.0
|
CG
|
A:HIS66
|
4.0
|
32.4
|
1.0
|
CB
|
A:ASP63
|
4.0
|
27.1
|
1.0
|
CG
|
B:GLU17
|
4.1
|
24.7
|
1.0
|
OE1
|
B:GLU21
|
4.2
|
31.4
|
1.0
|
CG
|
A:LYS65
|
4.3
|
43.3
|
1.0
|
CD
|
A:LYS65
|
4.3
|
44.6
|
1.0
|
NE2
|
A:HIS59
|
4.4
|
43.1
|
1.0
|
CE
|
A:LYS65
|
4.5
|
38.9
|
1.0
|
O
|
B:GLU17
|
4.7
|
19.0
|
1.0
|
CB
|
B:GLU21
|
4.9
|
20.0
|
1.0
|
|
Zinc binding site 2 out
of 5 in 1b0n
Go back to
Zinc Binding Sites List in 1b0n
Zinc binding site 2 out
of 5 in the Sinr Protein/Sini Protein Complex
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Sinr Protein/Sini Protein Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn1002
b:43.8
occ:1.00
|
O
|
A:HOH1096
|
1.8
|
33.8
|
1.0
|
OE1
|
A:GLU97
|
1.9
|
30.7
|
1.0
|
OE2
|
A:GLU97
|
2.3
|
36.2
|
1.0
|
O
|
A:HOH1095
|
2.3
|
25.0
|
1.0
|
CD
|
A:GLU97
|
2.5
|
26.0
|
1.0
|
CG
|
A:GLU97
|
4.0
|
25.7
|
1.0
|
NZ
|
A:LYS93
|
4.2
|
41.6
|
1.0
|
CG
|
A:GLN94
|
4.5
|
30.9
|
1.0
|
O
|
A:HOH1040
|
4.5
|
38.6
|
1.0
|
CB
|
A:GLU97
|
4.7
|
25.4
|
1.0
|
CA
|
A:GLN94
|
4.7
|
24.8
|
1.0
|
|
Zinc binding site 3 out
of 5 in 1b0n
Go back to
Zinc Binding Sites List in 1b0n
Zinc binding site 3 out
of 5 in the Sinr Protein/Sini Protein Complex
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Sinr Protein/Sini Protein Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn1003
b:20.2
occ:1.00
|
OD2
|
B:ASP12
|
1.8
|
18.2
|
1.0
|
NZ
|
A:LYS92
|
2.1
|
16.0
|
1.0
|
OD2
|
A:ASP55
|
2.1
|
19.7
|
1.0
|
CG
|
A:ASP55
|
2.7
|
19.5
|
1.0
|
CG
|
B:ASP12
|
2.7
|
19.4
|
1.0
|
OD1
|
A:ASP55
|
2.9
|
19.2
|
1.0
|
CE
|
A:LYS92
|
2.9
|
16.4
|
1.0
|
OD1
|
B:ASP12
|
3.0
|
17.2
|
1.0
|
CB
|
B:ASP12
|
4.1
|
22.1
|
1.0
|
O
|
A:HOH1046
|
4.2
|
34.8
|
1.0
|
CB
|
A:ASP55
|
4.2
|
16.0
|
1.0
|
O
|
A:HOH1024
|
4.3
|
23.7
|
1.0
|
CD
|
A:LYS92
|
4.3
|
18.7
|
1.0
|
O
|
A:ASP55
|
4.5
|
20.9
|
1.0
|
O
|
A:HOH1026
|
4.6
|
29.1
|
1.0
|
CB
|
B:GLU14
|
4.8
|
16.6
|
1.0
|
O
|
B:HOH60
|
5.0
|
29.2
|
1.0
|
CD1
|
B:TRP15
|
5.0
|
18.4
|
1.0
|
|
Zinc binding site 4 out
of 5 in 1b0n
Go back to
Zinc Binding Sites List in 1b0n
Zinc binding site 4 out
of 5 in the Sinr Protein/Sini Protein Complex
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of Sinr Protein/Sini Protein Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn1004
b:26.7
occ:1.00
|
N
|
A:MET1
|
2.1
|
22.3
|
1.0
|
OE1
|
A:GLU64
|
2.1
|
27.3
|
1.0
|
O
|
A:MET1
|
2.2
|
19.1
|
1.0
|
O
|
A:HOH1081
|
2.2
|
32.6
|
1.0
|
CD
|
A:GLU64
|
2.9
|
30.0
|
1.0
|
OE2
|
A:GLU64
|
2.9
|
22.9
|
1.0
|
C
|
A:MET1
|
2.9
|
18.0
|
1.0
|
CA
|
A:MET1
|
3.0
|
21.8
|
1.0
|
CB
|
A:MET1
|
3.9
|
21.8
|
1.0
|
O
|
A:HOH1051
|
4.1
|
35.2
|
1.0
|
NE2
|
A:GLN4
|
4.2
|
20.3
|
1.0
|
N
|
A:ILE2
|
4.2
|
19.4
|
1.0
|
CG
|
A:GLU64
|
4.4
|
27.9
|
1.0
|
O
|
A:HOH1048
|
4.5
|
47.2
|
1.0
|
CG
|
A:MET1
|
4.6
|
23.4
|
0.5
|
CG
|
A:GLU67
|
4.7
|
40.6
|
1.0
|
CB
|
A:GLU64
|
4.8
|
26.7
|
1.0
|
CG2
|
A:ILE2
|
4.8
|
25.5
|
1.0
|
CA
|
A:ILE2
|
4.9
|
23.6
|
1.0
|
OE1
|
A:GLN4
|
5.0
|
25.8
|
1.0
|
|
Zinc binding site 5 out
of 5 in 1b0n
Go back to
Zinc Binding Sites List in 1b0n
Zinc binding site 5 out
of 5 in the Sinr Protein/Sini Protein Complex
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 5 of Sinr Protein/Sini Protein Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn1005
b:38.4
occ:1.00
|
O
|
B:HOH79
|
1.6
|
19.7
|
1.0
|
O
|
B:HOH80
|
1.6
|
22.9
|
1.0
|
O
|
B:HOH78
|
1.9
|
23.3
|
1.0
|
OE2
|
B:GLU24
|
2.0
|
29.1
|
1.0
|
ND1
|
A:HIS66
|
2.0
|
31.6
|
1.0
|
CD
|
B:GLU24
|
2.8
|
28.4
|
1.0
|
OE1
|
B:GLU24
|
2.9
|
31.3
|
1.0
|
CE1
|
A:HIS66
|
3.0
|
32.9
|
1.0
|
CG
|
A:HIS66
|
3.1
|
32.4
|
1.0
|
CB
|
A:HIS66
|
3.4
|
33.6
|
1.0
|
CA
|
A:HIS66
|
3.7
|
33.0
|
1.0
|
CG1
|
B:VAL20
|
4.0
|
23.2
|
1.0
|
NE2
|
A:HIS66
|
4.1
|
30.3
|
1.0
|
CD2
|
A:HIS66
|
4.2
|
31.3
|
1.0
|
CG
|
B:GLU24
|
4.2
|
23.8
|
1.0
|
O
|
A:LYS65
|
4.4
|
39.4
|
1.0
|
N
|
A:HIS66
|
4.4
|
30.1
|
1.0
|
CG
|
A:LYS65
|
4.6
|
43.3
|
1.0
|
C
|
A:LYS65
|
4.7
|
34.9
|
1.0
|
CD
|
A:LYS65
|
4.9
|
44.6
|
1.0
|
C
|
A:HIS66
|
4.9
|
37.5
|
1.0
|
|
Reference:
R.J.Lewis,
J.A.Brannigan,
W.A.Offen,
I.Smith,
A.J.Wilkinson.
An Evolutionary Link Between Sporulation and Prophage Induction in the Structure of A Repressor:Anti-Repressor Complex. J.Mol.Biol. V. 283 907 1998.
ISSN: ISSN 0022-2836
PubMed: 9799632
DOI: 10.1006/JMBI.1998.2163
Page generated: Sat Oct 12 22:20:37 2024
|