Zinc in PDB 3l9x: Kefc C-Terminal Domain in Complex with Keff and Esg
Protein crystallography data
The structure of Kefc C-Terminal Domain in Complex with Keff and Esg, PDB code: 3l9x
was solved by
T.P.Roosild,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
38.26 /
2.10
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
64.949,
85.941,
189.408,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
20.3 /
23.6
|
Zinc Binding Sites:
The binding sites of Zinc atom in the Kefc C-Terminal Domain in Complex with Keff and Esg
(pdb code 3l9x). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the
Kefc C-Terminal Domain in Complex with Keff and Esg, PDB code: 3l9x:
Jump to Zinc binding site number:
1;
2;
Zinc binding site 1 out
of 2 in 3l9x
Go back to
Zinc Binding Sites List in 3l9x
Zinc binding site 1 out
of 2 in the Kefc C-Terminal Domain in Complex with Keff and Esg
 Mono view
 Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Kefc C-Terminal Domain in Complex with Keff and Esg within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn2402
b:47.6
occ:1.00
|
O
|
A:HOH85
|
3.1
|
21.8
|
1.0
|
N
|
A:HIS1012
|
3.2
|
28.7
|
1.0
|
CB
|
A:HIS1012
|
3.4
|
29.6
|
1.0
|
CA
|
A:TYR1010
|
3.5
|
22.5
|
1.0
|
C
|
A:TYR1010
|
3.5
|
23.2
|
1.0
|
N
|
A:PRO1011
|
3.6
|
24.1
|
1.0
|
CG
|
A:HIS1012
|
3.6
|
30.5
|
1.0
|
CD
|
A:PRO1011
|
3.7
|
23.7
|
1.0
|
CA
|
B:GLY536
|
3.7
|
23.0
|
1.0
|
CD2
|
A:HIS1013
|
3.8
|
37.0
|
1.0
|
CA
|
A:HIS1012
|
3.9
|
29.6
|
1.0
|
CB
|
A:TYR1010
|
3.9
|
22.2
|
1.0
|
CD2
|
A:HIS1012
|
4.1
|
32.3
|
1.0
|
N
|
B:GLY536
|
4.1
|
23.0
|
1.0
|
O
|
A:TYR1010
|
4.1
|
24.4
|
1.0
|
ND1
|
A:HIS1012
|
4.2
|
32.7
|
1.0
|
C
|
A:PRO1011
|
4.3
|
27.8
|
1.0
|
N
|
A:HIS1013
|
4.3
|
29.5
|
1.0
|
O
|
A:HOH106
|
4.4
|
21.3
|
1.0
|
NE2
|
A:HIS1013
|
4.4
|
40.1
|
1.0
|
CA
|
A:PRO1011
|
4.4
|
25.7
|
1.0
|
CD1
|
A:TYR1010
|
4.5
|
23.3
|
1.0
|
C
|
A:HIS1012
|
4.6
|
29.8
|
1.0
|
OE1
|
B:GLU539
|
4.6
|
29.0
|
1.0
|
O
|
A:PRO1009
|
4.7
|
20.8
|
1.0
|
CG
|
A:TYR1010
|
4.7
|
23.5
|
1.0
|
N
|
A:TYR1010
|
4.8
|
21.7
|
1.0
|
CG
|
A:PRO1011
|
4.8
|
24.2
|
1.0
|
NE2
|
A:HIS1012
|
4.8
|
30.9
|
1.0
|
CE1
|
A:HIS1012
|
4.8
|
30.8
|
1.0
|
CG
|
A:HIS1013
|
4.9
|
34.3
|
1.0
|
CB
|
A:PRO1011
|
4.9
|
25.7
|
1.0
|
C
|
B:GLY536
|
4.9
|
22.8
|
1.0
|
CB
|
B:GLU539
|
5.0
|
22.2
|
1.0
|
|
Zinc binding site 2 out
of 2 in 3l9x
Go back to
Zinc Binding Sites List in 3l9x
Zinc binding site 2 out
of 2 in the Kefc C-Terminal Domain in Complex with Keff and Esg
 Mono view
 Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Kefc C-Terminal Domain in Complex with Keff and Esg within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn2402
b:44.0
occ:1.00
|
O
|
A:HOH50
|
3.0
|
19.8
|
1.0
|
O
|
B:HOH274
|
3.0
|
22.9
|
1.0
|
N
|
B:HIS1012
|
3.4
|
25.4
|
1.0
|
CB
|
B:HIS1012
|
3.5
|
27.3
|
1.0
|
CA
|
B:TYR1010
|
3.5
|
20.3
|
1.0
|
C
|
B:TYR1010
|
3.5
|
20.5
|
1.0
|
CG
|
B:HIS1012
|
3.6
|
31.0
|
1.0
|
N
|
B:PRO1011
|
3.7
|
21.3
|
1.0
|
CD
|
B:PRO1011
|
3.8
|
20.2
|
1.0
|
ND1
|
B:HIS1012
|
3.8
|
32.6
|
1.0
|
CA
|
A:GLY536
|
3.9
|
19.0
|
1.0
|
CD2
|
B:HIS1013
|
3.9
|
34.6
|
1.0
|
CB
|
B:TYR1010
|
3.9
|
21.2
|
1.0
|
CA
|
B:HIS1012
|
4.0
|
27.4
|
1.0
|
O
|
B:TYR1010
|
4.0
|
19.6
|
1.0
|
O
|
B:HOH240
|
4.1
|
31.7
|
1.0
|
N
|
A:GLY536
|
4.1
|
19.8
|
1.0
|
NE2
|
B:HIS1013
|
4.4
|
35.1
|
1.0
|
C
|
B:PRO1011
|
4.4
|
24.3
|
1.0
|
CD2
|
B:HIS1012
|
4.4
|
33.8
|
1.0
|
CD1
|
B:TYR1010
|
4.4
|
22.8
|
1.0
|
OE1
|
A:GLU539
|
4.5
|
20.7
|
1.0
|
O
|
B:HOH67
|
4.5
|
18.2
|
1.0
|
N
|
B:HIS1013
|
4.5
|
26.9
|
1.0
|
CA
|
B:PRO1011
|
4.5
|
22.1
|
1.0
|
CE1
|
B:HIS1012
|
4.6
|
32.2
|
1.0
|
O
|
B:HOH147
|
4.7
|
37.8
|
1.0
|
CG
|
B:TYR1010
|
4.7
|
22.0
|
1.0
|
O
|
B:PRO1009
|
4.7
|
19.5
|
1.0
|
C
|
B:HIS1012
|
4.7
|
27.4
|
1.0
|
CG
|
B:PRO1011
|
4.8
|
21.7
|
1.0
|
N
|
B:TYR1010
|
4.8
|
19.9
|
1.0
|
CB
|
B:PRO1011
|
4.8
|
22.2
|
1.0
|
CB
|
A:GLU539
|
4.9
|
17.1
|
1.0
|
CG
|
B:HIS1013
|
4.9
|
31.6
|
1.0
|
NE2
|
B:HIS1012
|
4.9
|
33.7
|
1.0
|
C
|
A:GLY536
|
5.0
|
18.6
|
1.0
|
|
Reference:
T.P.Roosild,
S.Castronovo,
J.Healy,
S.Miller,
C.Pliotas,
T.Rasmussen,
W.Bartlett,
S.J.Conway,
I.R.Booth.
Mechanism of Ligand-Gated Potassium Efflux in Bacterial Pathogens. Proc.Natl.Acad.Sci.Usa V. 107 19784 2010.
ISSN: ISSN 0027-8424
PubMed: 21041667
DOI: 10.1073/PNAS.1012716107
Page generated: Sat Oct 26 08:26:58 2024
|