Zinc in PDB 2igi: Crystal Structure of E. Coli Oligoribonuclease
Protein crystallography data
The structure of Crystal Structure of E. Coli Oligoribonuclease, PDB code: 2igi
was solved by
Y.Zuo,
A.Malhotra,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
29.97 /
1.70
|
Space group
|
P 65
|
Cell size a, b, c (Å), α, β, γ (°)
|
91.550,
91.550,
111.180,
90.00,
90.00,
120.00
|
R / Rfree (%)
|
17.7 /
20
|
Other elements in 2igi:
The structure of Crystal Structure of E. Coli Oligoribonuclease also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of E. Coli Oligoribonuclease
(pdb code 2igi). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the
Crystal Structure of E. Coli Oligoribonuclease, PDB code: 2igi:
Jump to Zinc binding site number:
1;
2;
3;
4;
Zinc binding site 1 out
of 4 in 2igi
Go back to
Zinc Binding Sites List in 2igi
Zinc binding site 1 out
of 4 in the Crystal Structure of E. Coli Oligoribonuclease
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Crystal Structure of E. Coli Oligoribonuclease within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn1001
b:11.2
occ:1.00
|
OE2
|
A:GLU13
|
1.9
|
11.0
|
1.0
|
O
|
A:HOH1064
|
1.9
|
8.9
|
1.0
|
OD2
|
A:ASP162
|
2.0
|
11.2
|
1.0
|
OD2
|
A:ASP11
|
2.0
|
9.5
|
1.0
|
CD
|
A:GLU13
|
2.9
|
12.7
|
1.0
|
CG
|
A:ASP11
|
3.0
|
9.5
|
1.0
|
CG
|
A:ASP162
|
3.0
|
13.0
|
1.0
|
OD1
|
A:ASP11
|
3.2
|
8.6
|
1.0
|
ZN
|
A:ZN1004
|
3.3
|
14.1
|
1.0
|
CB
|
A:ASP162
|
3.3
|
10.7
|
1.0
|
CD
|
A:CD1002
|
3.4
|
11.1
|
1.0
|
OE1
|
A:GLU13
|
3.4
|
11.5
|
1.0
|
OXT
|
A:ACY603
|
3.6
|
16.3
|
1.0
|
O
|
A:LEU12
|
3.6
|
8.6
|
1.0
|
O
|
A:ACY603
|
3.7
|
20.6
|
1.0
|
C
|
A:ACY603
|
3.9
|
21.5
|
1.0
|
CA
|
A:HIS157
|
4.1
|
14.8
|
1.0
|
OD1
|
A:ASP162
|
4.1
|
13.8
|
1.0
|
CG
|
A:GLU13
|
4.2
|
11.2
|
1.0
|
C
|
A:HIS157
|
4.2
|
14.6
|
1.0
|
CA
|
A:ALA159
|
4.3
|
12.3
|
1.0
|
ND1
|
A:HIS157
|
4.3
|
12.6
|
1.0
|
CB
|
A:ASP11
|
4.3
|
8.4
|
1.0
|
O
|
A:HOH1100
|
4.3
|
11.1
|
1.0
|
O
|
A:GLN158
|
4.4
|
11.8
|
1.0
|
N
|
A:ALA159
|
4.4
|
11.9
|
1.0
|
C
|
A:GLN158
|
4.4
|
13.4
|
1.0
|
N
|
A:GLN158
|
4.4
|
14.3
|
1.0
|
C
|
A:LEU12
|
4.6
|
8.8
|
1.0
|
O
|
A:HIS157
|
4.7
|
13.8
|
1.0
|
CB
|
A:HIS157
|
4.7
|
14.7
|
1.0
|
OXT
|
A:ACY604
|
4.7
|
21.7
|
1.0
|
O
|
A:HOH1062
|
4.8
|
16.8
|
1.0
|
CA
|
A:ASP162
|
4.9
|
9.8
|
1.0
|
CG
|
A:HIS157
|
4.9
|
15.2
|
1.0
|
N
|
A:LEU12
|
5.0
|
8.7
|
1.0
|
O
|
A:ALA159
|
5.0
|
10.7
|
1.0
|
|
Zinc binding site 2 out
of 4 in 2igi
Go back to
Zinc Binding Sites List in 2igi
Zinc binding site 2 out
of 4 in the Crystal Structure of E. Coli Oligoribonuclease
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Crystal Structure of E. Coli Oligoribonuclease within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn1004
b:14.1
occ:1.00
|
OXT
|
A:ACY604
|
1.9
|
21.7
|
1.0
|
O
|
A:HOH1064
|
2.1
|
8.9
|
1.0
|
ND1
|
A:HIS157
|
2.1
|
12.6
|
1.0
|
OE1
|
A:GLU13
|
2.3
|
11.5
|
1.0
|
C
|
A:ACY604
|
2.6
|
24.4
|
1.0
|
O
|
A:ACY604
|
2.8
|
20.4
|
1.0
|
CE1
|
A:HIS157
|
2.9
|
14.2
|
1.0
|
CD
|
A:GLU13
|
3.2
|
12.7
|
1.0
|
CG
|
A:HIS157
|
3.2
|
15.2
|
1.0
|
ZN
|
A:ZN1001
|
3.3
|
11.2
|
1.0
|
OE2
|
A:GLU13
|
3.3
|
11.0
|
1.0
|
O
|
A:HOH1032
|
3.7
|
16.3
|
1.0
|
CB
|
A:HIS157
|
3.7
|
14.7
|
1.0
|
O
|
A:HOH1100
|
4.0
|
11.1
|
1.0
|
CD
|
A:CD1002
|
4.0
|
11.1
|
1.0
|
O
|
A:LEU12
|
4.0
|
8.6
|
1.0
|
O
|
A:ACY603
|
4.0
|
20.6
|
1.0
|
CH3
|
A:ACY604
|
4.1
|
24.2
|
1.0
|
NE2
|
A:HIS157
|
4.1
|
15.2
|
1.0
|
OD2
|
A:ASP162
|
4.3
|
11.2
|
1.0
|
CA
|
A:HIS157
|
4.3
|
14.8
|
1.0
|
CD2
|
A:HIS157
|
4.3
|
14.3
|
1.0
|
O
|
A:HOH1058
|
4.3
|
11.9
|
1.0
|
CG
|
A:GLU13
|
4.6
|
11.2
|
1.0
|
CA
|
A:GLU13
|
4.7
|
10.2
|
1.0
|
C
|
A:HIS157
|
4.9
|
14.6
|
1.0
|
C
|
A:ACY603
|
5.0
|
21.5
|
1.0
|
O
|
A:HIS157
|
5.0
|
13.8
|
1.0
|
|
Zinc binding site 3 out
of 4 in 2igi
Go back to
Zinc Binding Sites List in 2igi
Zinc binding site 3 out
of 4 in the Crystal Structure of E. Coli Oligoribonuclease
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Crystal Structure of E. Coli Oligoribonuclease within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn1007
b:11.7
occ:1.00
|
OE2
|
B:GLU13
|
1.9
|
11.2
|
1.0
|
O
|
B:HOH1063
|
1.9
|
10.6
|
1.0
|
OD2
|
B:ASP162
|
2.0
|
12.2
|
1.0
|
OD2
|
B:ASP11
|
2.0
|
9.4
|
1.0
|
CD
|
B:GLU13
|
2.9
|
12.3
|
1.0
|
CG
|
B:ASP162
|
3.0
|
13.5
|
1.0
|
CG
|
B:ASP11
|
3.0
|
10.1
|
1.0
|
OD1
|
B:ASP11
|
3.2
|
10.8
|
1.0
|
ZN
|
B:ZN1010
|
3.3
|
13.8
|
1.0
|
CB
|
B:ASP162
|
3.3
|
11.0
|
1.0
|
OE1
|
B:GLU13
|
3.4
|
10.7
|
1.0
|
CD
|
B:CD1008
|
3.4
|
11.4
|
1.0
|
OXT
|
B:ACY605
|
3.6
|
21.8
|
1.0
|
O
|
B:ACY605
|
3.7
|
17.4
|
1.0
|
O
|
B:LEU12
|
3.7
|
11.1
|
1.0
|
C
|
B:ACY605
|
4.0
|
23.1
|
1.0
|
CA
|
B:HIS157
|
4.1
|
12.8
|
1.0
|
OD1
|
B:ASP162
|
4.1
|
13.4
|
1.0
|
C
|
B:HIS157
|
4.2
|
13.7
|
1.0
|
CG
|
B:GLU13
|
4.2
|
10.9
|
1.0
|
CA
|
B:ALA159
|
4.3
|
13.6
|
1.0
|
N
|
B:ALA159
|
4.3
|
14.0
|
1.0
|
ND1
|
B:HIS157
|
4.3
|
13.9
|
1.0
|
CB
|
B:ASP11
|
4.4
|
10.0
|
1.0
|
O
|
B:HOH1079
|
4.4
|
10.0
|
1.0
|
N
|
B:GLN158
|
4.4
|
13.3
|
1.0
|
C
|
B:GLN158
|
4.4
|
14.0
|
1.0
|
O
|
B:GLN158
|
4.4
|
13.1
|
1.0
|
C
|
B:LEU12
|
4.6
|
10.5
|
1.0
|
O
|
B:HIS157
|
4.6
|
12.8
|
1.0
|
OXT
|
B:ACY606
|
4.6
|
20.8
|
1.0
|
CB
|
B:HIS157
|
4.7
|
13.6
|
1.0
|
O
|
B:HOH1037
|
4.7
|
16.4
|
1.0
|
CA
|
B:ASP162
|
4.8
|
11.9
|
1.0
|
CG
|
B:HIS157
|
4.9
|
14.6
|
1.0
|
O
|
B:ALA159
|
4.9
|
13.1
|
1.0
|
N
|
B:LEU12
|
5.0
|
11.3
|
1.0
|
|
Zinc binding site 4 out
of 4 in 2igi
Go back to
Zinc Binding Sites List in 2igi
Zinc binding site 4 out
of 4 in the Crystal Structure of E. Coli Oligoribonuclease
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of Crystal Structure of E. Coli Oligoribonuclease within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn1010
b:13.8
occ:1.00
|
OXT
|
B:ACY606
|
1.9
|
20.8
|
1.0
|
ND1
|
B:HIS157
|
2.1
|
13.9
|
1.0
|
O
|
B:HOH1063
|
2.1
|
10.6
|
1.0
|
OE1
|
B:GLU13
|
2.2
|
10.7
|
1.0
|
C
|
B:ACY606
|
2.7
|
22.5
|
1.0
|
O
|
B:ACY606
|
2.8
|
19.5
|
1.0
|
CE1
|
B:HIS157
|
2.9
|
15.0
|
1.0
|
CD
|
B:GLU13
|
3.1
|
12.3
|
1.0
|
CG
|
B:HIS157
|
3.2
|
14.6
|
1.0
|
ZN
|
B:ZN1007
|
3.3
|
11.7
|
1.0
|
OE2
|
B:GLU13
|
3.3
|
11.2
|
1.0
|
CB
|
B:HIS157
|
3.7
|
13.6
|
1.0
|
O
|
B:HOH1042
|
3.7
|
16.5
|
1.0
|
O
|
B:LEU12
|
4.0
|
11.1
|
1.0
|
CD
|
B:CD1008
|
4.0
|
11.4
|
1.0
|
O
|
B:HOH1079
|
4.0
|
10.0
|
1.0
|
OXT
|
B:ACY605
|
4.0
|
21.8
|
1.0
|
NE2
|
B:HIS157
|
4.1
|
15.3
|
1.0
|
CH3
|
B:ACY606
|
4.1
|
22.5
|
1.0
|
CA
|
B:HIS157
|
4.2
|
12.8
|
1.0
|
OD2
|
B:ASP162
|
4.2
|
12.2
|
1.0
|
CD2
|
B:HIS157
|
4.3
|
12.8
|
1.0
|
O
|
B:HOH1089
|
4.3
|
14.8
|
1.0
|
CG
|
B:GLU13
|
4.5
|
10.9
|
1.0
|
CA
|
B:GLU13
|
4.7
|
9.9
|
1.0
|
C
|
B:HIS157
|
4.9
|
13.7
|
1.0
|
O
|
B:HIS157
|
5.0
|
12.8
|
1.0
|
C
|
B:ACY605
|
5.0
|
23.1
|
1.0
|
CB
|
B:GLU13
|
5.0
|
11.4
|
1.0
|
|
Reference:
T.J.Fiedler,
Y.Zuo,
A.Malhotra.
Crystal Structure of Oligoribonuclease, the Lone Essential Exoribonuclease in Escherichia Coli To Be Published.
Page generated: Thu Oct 17 00:54:03 2024
|