Zinc in PDB 5zzu: Crystal Structure of the C-Terminal Periplasmic Domain of Eceptc From Escherichia Coli- Complex with Zn
Protein crystallography data
The structure of Crystal Structure of the C-Terminal Periplasmic Domain of Eceptc From Escherichia Coli- Complex with Zn, PDB code: 5zzu
was solved by
Y.Q.Zhao,
W.Cheng,
Y.J.Gu,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
46.83 /
2.10
|
Space group
|
P 32
|
Cell size a, b, c (Å), α, β, γ (°)
|
85.060,
85.060,
121.340,
90.00,
90.00,
120.00
|
R / Rfree (%)
|
16.5 /
19.7
|
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of the C-Terminal Periplasmic Domain of Eceptc From Escherichia Coli- Complex with Zn
(pdb code 5zzu). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the
Crystal Structure of the C-Terminal Periplasmic Domain of Eceptc From Escherichia Coli- Complex with Zn, PDB code: 5zzu:
Jump to Zinc binding site number:
1;
2;
3;
Zinc binding site 1 out
of 3 in 5zzu
Go back to
Zinc Binding Sites List in 5zzu
Zinc binding site 1 out
of 3 in the Crystal Structure of the C-Terminal Periplasmic Domain of Eceptc From Escherichia Coli- Complex with Zn
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 the C-Terminal Periplasmic Domain of Eceptc From Escherichia Coli- Complex with Zn within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn601
b:64.9
occ:1.00
|
O
|
A:ALA299
|
2.3
|
20.5
|
1.0
|
O
|
A:GLN294
|
2.4
|
22.9
|
1.0
|
O
|
A:ALA518
|
2.4
|
25.2
|
1.0
|
O
|
A:THR297
|
2.4
|
22.2
|
1.0
|
O
|
A:HOH770
|
2.5
|
16.8
|
1.0
|
O
|
A:HOH749
|
2.6
|
18.5
|
1.0
|
C
|
A:THR297
|
3.4
|
23.3
|
1.0
|
C
|
A:PHE298
|
3.4
|
21.8
|
1.0
|
C
|
A:ALA299
|
3.4
|
25.3
|
1.0
|
C
|
A:GLN294
|
3.5
|
24.4
|
1.0
|
N
|
A:ALA299
|
3.6
|
23.7
|
1.0
|
C
|
A:ALA518
|
3.6
|
22.5
|
1.0
|
CA
|
A:PHE298
|
3.7
|
20.8
|
1.0
|
O
|
A:PHE298
|
3.7
|
20.6
|
1.0
|
N
|
A:PHE298
|
4.0
|
22.4
|
1.0
|
CA
|
A:ALA299
|
4.1
|
24.6
|
1.0
|
CA
|
A:GLN294
|
4.1
|
22.1
|
1.0
|
CA
|
A:GLU519
|
4.4
|
22.8
|
1.0
|
N
|
A:THR297
|
4.4
|
20.8
|
1.0
|
N
|
A:GLU519
|
4.4
|
22.0
|
1.0
|
N
|
A:ALA295
|
4.5
|
22.3
|
1.0
|
N
|
A:ASN300
|
4.5
|
20.7
|
1.0
|
CG2
|
A:ILE521
|
4.5
|
21.5
|
1.0
|
CA
|
A:THR297
|
4.5
|
22.9
|
1.0
|
CA
|
A:ALA518
|
4.5
|
20.6
|
1.0
|
CB
|
A:GLN294
|
4.6
|
22.9
|
1.0
|
O
|
A:ALA295
|
4.6
|
24.8
|
1.0
|
OG1
|
A:THR297
|
4.6
|
21.4
|
1.0
|
CA
|
A:ALA295
|
4.6
|
22.9
|
1.0
|
OE1
|
A:GLU519
|
4.7
|
24.8
|
1.0
|
C
|
A:ALA295
|
4.7
|
20.7
|
1.0
|
CB
|
A:ASN300
|
4.8
|
21.9
|
1.0
|
CA
|
A:ASN300
|
4.8
|
24.6
|
1.0
|
C
|
A:GLU519
|
4.9
|
21.3
|
1.0
|
|
Zinc binding site 2 out
of 3 in 5zzu
Go back to
Zinc Binding Sites List in 5zzu
Zinc binding site 2 out
of 3 in the Crystal Structure of the C-Terminal Periplasmic Domain of Eceptc From Escherichia Coli- Complex with Zn
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 the C-Terminal Periplasmic Domain of Eceptc From Escherichia Coli- Complex with Zn within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn601
b:57.4
occ:1.00
|
O
|
B:GLN294
|
2.3
|
19.3
|
1.0
|
O
|
B:ALA518
|
2.4
|
23.8
|
1.0
|
O
|
B:THR297
|
2.4
|
18.6
|
1.0
|
O
|
B:HOH779
|
2.4
|
18.9
|
1.0
|
O
|
B:ALA299
|
2.4
|
26.6
|
1.0
|
O
|
B:HOH760
|
2.5
|
17.9
|
1.0
|
C
|
B:GLN294
|
3.4
|
19.8
|
1.0
|
C
|
B:THR297
|
3.4
|
18.9
|
1.0
|
C
|
B:PHE298
|
3.5
|
20.6
|
1.0
|
C
|
B:ALA299
|
3.5
|
26.1
|
1.0
|
C
|
B:ALA518
|
3.6
|
21.0
|
1.0
|
N
|
B:ALA299
|
3.7
|
22.9
|
1.0
|
CA
|
B:PHE298
|
3.8
|
19.6
|
1.0
|
O
|
B:PHE298
|
3.9
|
22.6
|
1.0
|
N
|
B:PHE298
|
4.0
|
23.6
|
1.0
|
CA
|
B:GLN294
|
4.1
|
20.3
|
1.0
|
CA
|
B:ALA299
|
4.2
|
26.8
|
1.0
|
N
|
B:ALA295
|
4.3
|
20.3
|
1.0
|
N
|
B:THR297
|
4.4
|
19.2
|
1.0
|
CG2
|
B:ILE521
|
4.4
|
19.4
|
1.0
|
CA
|
B:GLU519
|
4.4
|
19.3
|
1.0
|
N
|
B:GLU519
|
4.4
|
19.5
|
1.0
|
CA
|
B:ALA518
|
4.5
|
21.8
|
1.0
|
CA
|
B:THR297
|
4.5
|
22.3
|
1.0
|
CA
|
B:ALA295
|
4.5
|
22.0
|
1.0
|
CB
|
B:GLN294
|
4.5
|
16.3
|
1.0
|
O
|
B:ALA295
|
4.5
|
20.7
|
1.0
|
C
|
B:ALA295
|
4.5
|
20.3
|
1.0
|
N
|
B:ASN300
|
4.6
|
23.5
|
1.0
|
OG1
|
B:THR297
|
4.6
|
21.5
|
1.0
|
OE1
|
B:GLU519
|
4.7
|
27.1
|
1.0
|
CB
|
B:ASN300
|
4.9
|
25.9
|
1.0
|
C
|
B:GLU519
|
4.9
|
21.4
|
1.0
|
CA
|
B:ASN300
|
4.9
|
25.1
|
1.0
|
N
|
B:LEU520
|
4.9
|
20.9
|
1.0
|
|
Zinc binding site 3 out
of 3 in 5zzu
Go back to
Zinc Binding Sites List in 5zzu
Zinc binding site 3 out
of 3 in the Crystal Structure of the C-Terminal Periplasmic Domain of Eceptc From Escherichia Coli- Complex with Zn
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 the C-Terminal Periplasmic Domain of Eceptc From Escherichia Coli- Complex with Zn within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn601
b:55.5
occ:1.00
|
O
|
C:GLN294
|
2.4
|
19.9
|
1.0
|
O
|
C:THR297
|
2.4
|
22.5
|
1.0
|
O
|
C:ALA518
|
2.4
|
24.6
|
1.0
|
O
|
C:ALA299
|
2.4
|
19.8
|
1.0
|
O
|
C:HOH806
|
2.5
|
21.7
|
1.0
|
O
|
C:HOH720
|
2.8
|
18.6
|
1.0
|
C
|
C:THR297
|
3.4
|
23.2
|
1.0
|
C
|
C:GLN294
|
3.4
|
19.3
|
1.0
|
C
|
C:PHE298
|
3.5
|
19.2
|
1.0
|
C
|
C:ALA299
|
3.5
|
21.4
|
1.0
|
C
|
C:ALA518
|
3.6
|
26.7
|
1.0
|
N
|
C:ALA299
|
3.6
|
20.4
|
1.0
|
CA
|
C:PHE298
|
3.7
|
19.9
|
1.0
|
O
|
C:PHE298
|
3.9
|
23.4
|
1.0
|
N
|
C:PHE298
|
4.0
|
20.0
|
1.0
|
CA
|
C:GLN294
|
4.1
|
20.1
|
1.0
|
CA
|
C:ALA299
|
4.2
|
23.0
|
1.0
|
N
|
C:ALA295
|
4.4
|
20.7
|
1.0
|
N
|
C:THR297
|
4.4
|
18.6
|
1.0
|
CG2
|
C:ILE521
|
4.4
|
21.2
|
1.0
|
CA
|
C:GLU519
|
4.5
|
25.2
|
1.0
|
N
|
C:GLU519
|
4.5
|
21.6
|
1.0
|
CA
|
C:ALA518
|
4.5
|
24.5
|
1.0
|
CB
|
C:GLN294
|
4.5
|
20.1
|
1.0
|
CA
|
C:THR297
|
4.5
|
23.4
|
1.0
|
N
|
C:ASN300
|
4.5
|
22.1
|
1.0
|
CA
|
C:ALA295
|
4.6
|
22.5
|
1.0
|
O
|
C:ALA295
|
4.6
|
21.5
|
1.0
|
C
|
C:ALA295
|
4.6
|
20.7
|
1.0
|
OG1
|
C:THR297
|
4.7
|
21.6
|
1.0
|
CB
|
C:ASN300
|
4.8
|
21.8
|
1.0
|
OE1
|
C:GLU519
|
4.8
|
26.1
|
1.0
|
CA
|
C:ASN300
|
4.8
|
22.5
|
1.0
|
C
|
C:GLU519
|
4.9
|
22.8
|
1.0
|
|
Reference:
Y.Q.Zhao,
Y.J.Lai,
D.Zhou,
C.Dou,
Y.J.Gu,
C.L.Nie,
Y.Q.Wei,
W.Cheng.
Structural and Mechanistic Insights Into Polymyxin Resistance Mediated By Eptc Originating From Escherichia Coli To Be Published.
Page generated: Mon Oct 28 17:13:24 2024
|