Potassium in PDB 5tao: Haloferax Volcanii Malate Synthase Lead(II) Complex
Enzymatic activity of Haloferax Volcanii Malate Synthase Lead(II) Complex
All present enzymatic activity of Haloferax Volcanii Malate Synthase Lead(II) Complex:
2.3.3.9;
Protein crystallography data
The structure of Haloferax Volcanii Malate Synthase Lead(II) Complex, PDB code: 5tao
was solved by
B.R.Howard,
M.J.Adams,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
96.81 /
2.10
|
Space group
|
H 3 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
155.353,
155.353,
139.412,
90.00,
90.00,
120.00
|
R / Rfree (%)
|
18.3 /
21.7
|
Other elements in 5tao:
The structure of Haloferax Volcanii Malate Synthase Lead(II) Complex also contains other interesting chemical elements:
Potassium Binding Sites:
The binding sites of Potassium atom in the Haloferax Volcanii Malate Synthase Lead(II) Complex
(pdb code 5tao). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total 3 binding sites of Potassium where determined in the
Haloferax Volcanii Malate Synthase Lead(II) Complex, PDB code: 5tao:
Jump to Potassium binding site number:
1;
2;
3;
Potassium binding site 1 out
of 3 in 5tao
Go back to
Potassium Binding Sites List in 5tao
Potassium binding site 1 out
of 3 in the Haloferax Volcanii Malate Synthase Lead(II) Complex
 Mono view
 Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 1 of Haloferax Volcanii Malate Synthase Lead(II) Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K509
b:32.0
occ:1.00
|
OXT
|
A:ACT501
|
2.5
|
66.4
|
1.0
|
O
|
A:LYS175
|
2.6
|
41.4
|
1.0
|
O
|
A:ASN178
|
2.6
|
27.8
|
1.0
|
O
|
A:MET173
|
2.7
|
36.6
|
1.0
|
OE1
|
A:GLU181
|
2.8
|
36.1
|
1.0
|
OE2
|
A:GLU181
|
2.9
|
59.1
|
1.0
|
OD1
|
A:ASN178
|
2.9
|
31.8
|
1.0
|
CD
|
A:GLU181
|
3.1
|
53.5
|
1.0
|
C
|
A:ACT501
|
3.3
|
78.2
|
1.0
|
O
|
A:ACT501
|
3.3
|
70.8
|
1.0
|
C
|
A:ASN178
|
3.5
|
28.5
|
1.0
|
C
|
A:LYS175
|
3.7
|
37.9
|
1.0
|
C
|
A:MET173
|
3.7
|
37.5
|
1.0
|
C
|
A:GLY174
|
3.8
|
41.4
|
1.0
|
CG
|
A:ASN178
|
3.9
|
31.0
|
1.0
|
N
|
A:LYS175
|
4.0
|
40.0
|
1.0
|
O
|
A:GLY174
|
4.0
|
38.9
|
1.0
|
CA
|
A:GLY174
|
4.1
|
39.7
|
1.0
|
N
|
A:LEU180
|
4.2
|
34.2
|
1.0
|
N
|
A:ASN179
|
4.2
|
29.8
|
1.0
|
CA
|
A:ASN179
|
4.3
|
30.6
|
1.0
|
CA
|
A:ASN178
|
4.4
|
28.9
|
1.0
|
N
|
A:GLY174
|
4.4
|
44.3
|
1.0
|
K
|
A:K511
|
4.5
|
51.6
|
1.0
|
CA
|
A:LYS175
|
4.5
|
35.9
|
1.0
|
N
|
A:ASN178
|
4.5
|
30.7
|
1.0
|
CG
|
A:GLU181
|
4.5
|
48.9
|
1.0
|
C
|
A:ASN179
|
4.6
|
35.5
|
1.0
|
ND2
|
A:ASN178
|
4.6
|
30.1
|
1.0
|
CH3
|
A:ACT501
|
4.7
|
78.7
|
1.0
|
N
|
A:PRO176
|
4.7
|
39.3
|
1.0
|
CA
|
A:PRO176
|
4.7
|
41.6
|
1.0
|
CB
|
A:ASN178
|
4.7
|
29.9
|
1.0
|
CA
|
A:MET173
|
4.7
|
37.0
|
1.0
|
N
|
A:GLU181
|
4.9
|
31.5
|
1.0
|
|
Potassium binding site 2 out
of 3 in 5tao
Go back to
Potassium Binding Sites List in 5tao
Potassium binding site 2 out
of 3 in the Haloferax Volcanii Malate Synthase Lead(II) Complex
 Mono view
 Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 2 of Haloferax Volcanii Malate Synthase Lead(II) Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K510
b:37.0
occ:1.00
|
OG
|
A:SER221
|
2.7
|
32.3
|
0.5
|
OG
|
A:SER217
|
2.8
|
34.0
|
1.0
|
O
|
A:HOH601
|
2.8
|
39.5
|
0.5
|
O
|
A:GLY252
|
2.9
|
31.1
|
1.0
|
O
|
A:SER217
|
3.1
|
29.2
|
1.0
|
CL
|
A:CL514
|
3.2
|
37.2
|
1.0
|
C
|
A:GLY252
|
3.7
|
32.1
|
1.0
|
C
|
A:SER217
|
3.7
|
32.4
|
1.0
|
CB
|
A:SER217
|
3.9
|
36.1
|
1.0
|
O
|
A:HOH714
|
3.9
|
72.4
|
1.0
|
CA
|
A:SER217
|
3.9
|
31.4
|
1.0
|
CB
|
A:SER221
|
4.1
|
33.5
|
0.5
|
CA
|
A:GLY252
|
4.2
|
33.4
|
1.0
|
N
|
A:SER221
|
4.4
|
31.9
|
0.5
|
N
|
A:SER221
|
4.4
|
30.8
|
0.5
|
CB
|
A:SER221
|
4.6
|
35.7
|
0.5
|
O
|
A:LYS251
|
4.6
|
36.0
|
1.0
|
CB
|
A:ALA220
|
4.7
|
30.9
|
1.0
|
CB
|
A:ALA227
|
4.7
|
29.1
|
1.0
|
CA
|
A:SER221
|
4.8
|
35.2
|
0.5
|
CA
|
A:SER221
|
4.8
|
32.6
|
0.5
|
N
|
A:MET253
|
4.8
|
36.3
|
1.0
|
N
|
A:ARG218
|
4.9
|
32.0
|
1.0
|
|
Potassium binding site 3 out
of 3 in 5tao
Go back to
Potassium Binding Sites List in 5tao
Potassium binding site 3 out
of 3 in the Haloferax Volcanii Malate Synthase Lead(II) Complex
 Mono view
 Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 3 of Haloferax Volcanii Malate Synthase Lead(II) Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K511
b:51.6
occ:1.00
|
O
|
A:ACT501
|
2.4
|
70.8
|
1.0
|
O
|
A:ASN178
|
2.6
|
27.8
|
1.0
|
OD1
|
A:ASN179
|
2.8
|
34.0
|
1.0
|
O
|
A:PRO176
|
3.0
|
36.5
|
1.0
|
C
|
A:ACT501
|
3.4
|
78.2
|
1.0
|
C
|
A:ASN178
|
3.4
|
28.5
|
1.0
|
O
|
A:HOH812
|
3.5
|
50.4
|
1.0
|
CG
|
A:ASN179
|
3.7
|
34.8
|
1.0
|
C
|
A:PRO176
|
3.9
|
36.9
|
1.0
|
N
|
A:ASN178
|
4.1
|
30.7
|
1.0
|
CH3
|
A:ACT501
|
4.1
|
78.7
|
1.0
|
N
|
A:ASN179
|
4.2
|
29.8
|
1.0
|
O
|
A:HOH696
|
4.2
|
47.2
|
1.0
|
ND2
|
A:ASN179
|
4.3
|
42.8
|
1.0
|
OXT
|
A:ACT501
|
4.3
|
66.4
|
1.0
|
CA
|
A:ASN178
|
4.3
|
28.9
|
1.0
|
CA
|
A:ASN179
|
4.3
|
30.6
|
1.0
|
CA
|
A:PRO176
|
4.4
|
41.6
|
1.0
|
K
|
A:K509
|
4.5
|
32.0
|
1.0
|
CB
|
A:ASN179
|
4.6
|
31.8
|
1.0
|
O
|
A:LYS175
|
4.7
|
41.4
|
1.0
|
C
|
A:THR177
|
4.7
|
32.8
|
1.0
|
N
|
A:THR177
|
4.8
|
33.5
|
1.0
|
|
Reference:
M.J.Adams,
B.R.Howard.
X-Ray Analysis of Lead(II) Binding to Haloferax Volcanii Malate Synthase The Journal of the Utah V. 93 77 2016ACADEMY.
ISSN: ISSN 0083-4823
Page generated: Mon Aug 12 14:33:15 2024
|