Zinc in PDB 4km4: E. Coli Alkaline Phosphatase Mutant S102G/R166S in Complex with Inorganic Phosphate
Enzymatic activity of E. Coli Alkaline Phosphatase Mutant S102G/R166S in Complex with Inorganic Phosphate
All present enzymatic activity of E. Coli Alkaline Phosphatase Mutant S102G/R166S in Complex with Inorganic Phosphate:
3.1.3.1;
Protein crystallography data
The structure of E. Coli Alkaline Phosphatase Mutant S102G/R166S in Complex with Inorganic Phosphate, PDB code: 4km4
was solved by
L.D.Andrews,
T.D.Fenn,
D.Herschlag,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
|
Resolution Low / High (Å)
|
50.00 /
2.80
|
|
Space group
|
P 63 2 2
|
|
Cell size a, b, c (Å), α, β, γ (°)
|
160.935,
160.935,
139.549,
90.00,
90.00,
120.00
|
|
R / Rfree (%)
|
23.2 /
29.6
|
Zinc Binding Sites:
The binding sites of Zinc atom in the E. Coli Alkaline Phosphatase Mutant S102G/R166S in Complex with Inorganic Phosphate
(pdb code 4km4). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 6 binding sites of Zinc where determined in the
E. Coli Alkaline Phosphatase Mutant S102G/R166S in Complex with Inorganic Phosphate, PDB code: 4km4:
Jump to Zinc binding site number:
1;
2;
3;
4;
5;
6;
Zinc binding site 1 out
of 6 in 4km4
Go back to
Zinc Binding Sites List in 4km4
Zinc binding site 1 out
of 6 in the E. Coli Alkaline Phosphatase Mutant S102G/R166S in Complex with Inorganic Phosphate
 Mono view
 Stereo pair view
|
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of E. Coli Alkaline Phosphatase Mutant S102G/R166S in Complex with Inorganic Phosphate within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn502
b:13.9
occ:1.00
|
OD1
|
A:ASP51
|
1.9
|
18.8
|
1.0
|
|
OD2
|
A:ASP369
|
1.9
|
10.2
|
1.0
|
|
NE2
|
A:HIS370
|
2.0
|
4.3
|
1.0
|
|
O2
|
A:PO4501
|
2.1
|
4.5
|
1.0
|
|
CG
|
A:ASP51
|
2.8
|
17.1
|
1.0
|
|
CG
|
A:ASP369
|
2.8
|
8.6
|
1.0
|
|
CD2
|
A:HIS370
|
2.9
|
6.0
|
1.0
|
|
HD2
|
A:HIS370
|
3.0
|
6.0
|
1.0
|
|
OD1
|
A:ASP369
|
3.0
|
5.5
|
1.0
|
|
OD2
|
A:ASP51
|
3.1
|
16.1
|
1.0
|
|
CE1
|
A:HIS370
|
3.1
|
8.1
|
1.0
|
|
OD1
|
A:ASP327
|
3.5
|
18.1
|
1.0
|
|
HE1
|
A:HIS370
|
3.5
|
8.1
|
1.0
|
|
HA2
|
A:GLY102
|
3.5
|
11.3
|
1.0
|
|
HA3
|
A:GLY102
|
3.5
|
11.3
|
1.0
|
|
P
|
A:PO4501
|
3.5
|
11.7
|
1.0
|
|
H
|
A:GLY52
|
3.6
|
14.2
|
1.0
|
|
HE1
|
A:HIS412
|
3.6
|
10.9
|
1.0
|
|
O3
|
A:PO4501
|
3.9
|
15.1
|
1.0
|
|
HB2
|
A:ASP327
|
3.9
|
15.7
|
1.0
|
|
CA
|
A:GLY102
|
3.9
|
11.3
|
1.0
|
|
CG
|
A:ASP327
|
3.9
|
17.7
|
1.0
|
|
HA
|
A:ASP51
|
4.0
|
14.3
|
1.0
|
|
CE1
|
A:HIS412
|
4.1
|
10.9
|
1.0
|
|
ZN
|
A:ZN503
|
4.1
|
14.6
|
1.0
|
|
CG
|
A:HIS370
|
4.1
|
7.2
|
1.0
|
|
CB
|
A:ASP51
|
4.1
|
16.9
|
1.0
|
|
ND1
|
A:HIS370
|
4.2
|
8.6
|
1.0
|
|
N
|
A:GLY52
|
4.2
|
14.2
|
1.0
|
|
CB
|
A:ASP369
|
4.2
|
7.6
|
1.0
|
|
N
|
A:GLY102
|
4.3
|
8.5
|
1.0
|
|
O1
|
A:PO4501
|
4.3
|
6.9
|
1.0
|
|
H
|
A:GLY102
|
4.3
|
8.5
|
1.0
|
|
NE2
|
A:HIS412
|
4.3
|
11.7
|
1.0
|
|
CB
|
A:ASP327
|
4.4
|
15.7
|
1.0
|
|
HB3
|
A:ASP327
|
4.4
|
15.7
|
1.0
|
|
CA
|
A:ASP51
|
4.4
|
14.3
|
1.0
|
|
HB2
|
A:ASP369
|
4.4
|
7.6
|
1.0
|
|
O4
|
A:PO4501
|
4.5
|
17.8
|
1.0
|
|
OD2
|
A:ASP327
|
4.5
|
18.4
|
1.0
|
|
C
|
A:ASP51
|
4.6
|
14.7
|
1.0
|
|
HB3
|
A:ASP369
|
4.7
|
7.6
|
1.0
|
|
HB3
|
A:ASP51
|
4.7
|
16.9
|
1.0
|
|
HG1
|
A:THR155
|
4.7
|
14.6
|
1.0
|
|
H
|
A:HIS370
|
4.7
|
8.6
|
1.0
|
|
ZN
|
A:ZN504
|
4.8
|
21.2
|
1.0
|
|
HA2
|
A:GLY52
|
4.8
|
13.9
|
1.0
|
|
HB2
|
A:ASP51
|
4.9
|
16.9
|
1.0
|
|
ND1
|
A:HIS412
|
4.9
|
12.3
|
1.0
|
|
C
|
A:ASP101
|
5.0
|
8.6
|
1.0
|
|
Zinc binding site 2 out
of 6 in 4km4
Go back to
Zinc Binding Sites List in 4km4
Zinc binding site 2 out
of 6 in the E. Coli Alkaline Phosphatase Mutant S102G/R166S in Complex with Inorganic Phosphate
 Mono view
 Stereo pair view
|
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of E. Coli Alkaline Phosphatase Mutant S102G/R166S in Complex with Inorganic Phosphate within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn503
b:14.6
occ:1.00
|
OD1
|
A:ASP327
|
1.9
|
18.1
|
1.0
|
|
NE2
|
A:HIS331
|
2.0
|
7.2
|
1.0
|
|
NE2
|
A:HIS412
|
2.0
|
11.7
|
1.0
|
|
O1
|
A:PO4501
|
2.2
|
6.9
|
1.0
|
|
CG
|
A:ASP327
|
2.7
|
17.7
|
1.0
|
|
OD2
|
A:ASP327
|
2.8
|
18.4
|
1.0
|
|
CD2
|
A:HIS331
|
3.0
|
7.3
|
1.0
|
|
CE1
|
A:HIS412
|
3.0
|
10.9
|
1.0
|
|
CD2
|
A:HIS412
|
3.0
|
13.1
|
1.0
|
|
CE1
|
A:HIS331
|
3.0
|
3.7
|
1.0
|
|
HD2
|
A:HIS331
|
3.1
|
7.3
|
1.0
|
|
O2
|
A:PO4501
|
3.1
|
4.5
|
1.0
|
|
HE1
|
A:HIS412
|
3.2
|
10.9
|
1.0
|
|
HD2
|
A:HIS412
|
3.2
|
13.1
|
1.0
|
|
P
|
A:PO4501
|
3.3
|
11.7
|
1.0
|
|
HE1
|
A:HIS331
|
3.4
|
3.7
|
1.0
|
|
HE1
|
A:HIS370
|
3.5
|
8.1
|
1.0
|
|
NE2
|
A:HIS372
|
3.8
|
10.0
|
1.0
|
|
CE1
|
A:HIS370
|
4.0
|
8.1
|
1.0
|
|
NE2
|
A:HIS370
|
4.1
|
4.3
|
1.0
|
|
ZN
|
A:ZN502
|
4.1
|
13.9
|
1.0
|
|
ND1
|
A:HIS412
|
4.1
|
12.3
|
1.0
|
|
ND1
|
A:HIS331
|
4.2
|
4.9
|
1.0
|
|
CG
|
A:HIS331
|
4.2
|
6.8
|
1.0
|
|
CB
|
A:ASP327
|
4.2
|
15.7
|
1.0
|
|
CG
|
A:HIS412
|
4.2
|
12.7
|
1.0
|
|
HD2
|
A:HIS372
|
4.3
|
9.2
|
1.0
|
|
O4
|
A:PO4501
|
4.3
|
17.8
|
1.0
|
|
O3
|
A:PO4501
|
4.3
|
15.1
|
1.0
|
|
CD2
|
A:HIS372
|
4.4
|
9.2
|
1.0
|
|
HB2
|
A:ASP327
|
4.4
|
15.7
|
1.0
|
|
OD1
|
A:ASP51
|
4.7
|
18.8
|
1.0
|
|
HZ2
|
A:LYS328
|
4.7
|
22.3
|
1.0
|
|
CE1
|
A:HIS372
|
4.7
|
10.1
|
1.0
|
|
HB3
|
A:ASP327
|
4.7
|
15.7
|
1.0
|
|
O
|
A:ASP327
|
4.9
|
10.9
|
1.0
|
|
HE1
|
A:HIS372
|
5.0
|
10.1
|
1.0
|
|
Zinc binding site 3 out
of 6 in 4km4
Go back to
Zinc Binding Sites List in 4km4
Zinc binding site 3 out
of 6 in the E. Coli Alkaline Phosphatase Mutant S102G/R166S in Complex with Inorganic Phosphate
 Mono view
 Stereo pair view
|
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of E. Coli Alkaline Phosphatase Mutant S102G/R166S in Complex with Inorganic Phosphate within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn504
b:21.2
occ:1.00
|
OE2
|
A:GLU322
|
1.9
|
16.6
|
1.0
|
|
OD2
|
A:ASP51
|
1.9
|
16.1
|
1.0
|
|
OD2
|
A:ASP153
|
2.0
|
34.1
|
1.0
|
|
OG1
|
A:THR155
|
2.0
|
14.6
|
1.0
|
|
HG1
|
A:THR155
|
2.6
|
14.6
|
1.0
|
|
CD
|
A:GLU322
|
2.9
|
18.1
|
1.0
|
|
CG
|
A:ASP51
|
3.1
|
17.1
|
1.0
|
|
HB
|
A:THR155
|
3.1
|
14.8
|
1.0
|
|
CB
|
A:THR155
|
3.1
|
14.8
|
1.0
|
|
H
|
A:THR155
|
3.2
|
16.1
|
1.0
|
|
CG
|
A:ASP153
|
3.2
|
32.9
|
1.0
|
|
OE1
|
A:GLU322
|
3.2
|
19.2
|
1.0
|
|
HB2
|
A:ASP51
|
3.4
|
16.9
|
1.0
|
|
HB1
|
A:ALA324
|
3.6
|
17.0
|
1.0
|
|
OD1
|
A:ASP153
|
3.7
|
32.8
|
1.0
|
|
O3
|
A:PO4501
|
3.7
|
15.1
|
1.0
|
|
CB
|
A:ASP51
|
3.8
|
16.9
|
1.0
|
|
HZ1
|
A:LYS328
|
3.8
|
22.3
|
1.0
|
|
HG21
|
A:THR155
|
3.9
|
14.5
|
1.0
|
|
N
|
A:THR155
|
4.0
|
16.1
|
1.0
|
|
HE2
|
A:LYS328
|
4.0
|
18.6
|
1.0
|
|
HA
|
A:ALA324
|
4.0
|
17.6
|
1.0
|
|
CG2
|
A:THR155
|
4.1
|
14.5
|
1.0
|
|
OD1
|
A:ASP51
|
4.1
|
18.8
|
1.0
|
|
HD2
|
A:PRO156
|
4.1
|
20.4
|
1.0
|
|
CA
|
A:THR155
|
4.1
|
16.1
|
1.0
|
|
HB3
|
A:ASP51
|
4.2
|
16.9
|
1.0
|
|
HB2
|
A:ALA154
|
4.2
|
13.1
|
1.0
|
|
CG
|
A:GLU322
|
4.2
|
17.4
|
1.0
|
|
HZ2
|
A:LYS328
|
4.3
|
22.3
|
1.0
|
|
HG3
|
A:GLU322
|
4.3
|
17.4
|
1.0
|
|
CB
|
A:ALA324
|
4.4
|
17.0
|
1.0
|
|
NZ
|
A:LYS328
|
4.4
|
22.3
|
1.0
|
|
HB3
|
A:ALA324
|
4.5
|
17.0
|
1.0
|
|
CB
|
A:ASP153
|
4.5
|
29.3
|
1.0
|
|
HB3
|
A:ASP153
|
4.5
|
29.3
|
1.0
|
|
HG2
|
A:GLU322
|
4.6
|
17.4
|
1.0
|
|
HG22
|
A:THR155
|
4.7
|
14.5
|
1.0
|
|
HB2
|
A:ALA149
|
4.7
|
19.6
|
1.0
|
|
HB3
|
A:ALA149
|
4.7
|
19.6
|
1.0
|
|
H
|
A:ALA154
|
4.7
|
15.6
|
1.0
|
|
CE
|
A:LYS328
|
4.7
|
18.6
|
1.0
|
|
HD3
|
A:PRO156
|
4.7
|
20.4
|
1.0
|
|
CA
|
A:ALA324
|
4.7
|
17.6
|
1.0
|
|
HA
|
A:THR155
|
4.7
|
16.1
|
1.0
|
|
ZN
|
A:ZN502
|
4.8
|
13.9
|
1.0
|
|
O
|
A:ALA324
|
4.8
|
20.8
|
1.0
|
|
HA3
|
A:GLY102
|
4.9
|
11.3
|
1.0
|
|
OD2
|
A:ASP369
|
4.9
|
10.2
|
1.0
|
|
HG
|
A:SER147
|
4.9
|
14.5
|
1.0
|
|
CD
|
A:PRO156
|
5.0
|
20.4
|
1.0
|
|
N
|
A:ALA154
|
5.0
|
15.6
|
1.0
|
|
HG23
|
A:THR155
|
5.0
|
14.5
|
1.0
|
|
Zinc binding site 4 out
of 6 in 4km4
Go back to
Zinc Binding Sites List in 4km4
Zinc binding site 4 out
of 6 in the E. Coli Alkaline Phosphatase Mutant S102G/R166S in Complex with Inorganic Phosphate
 Mono view
 Stereo pair view
|
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of E. Coli Alkaline Phosphatase Mutant S102G/R166S in Complex with Inorganic Phosphate within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn502
b:10.8
occ:1.00
|
OD1
|
B:ASP51
|
1.8
|
9.7
|
1.0
|
|
OD2
|
B:ASP369
|
1.9
|
21.5
|
1.0
|
|
NE2
|
B:HIS370
|
2.0
|
14.2
|
1.0
|
|
O2
|
B:PO4501
|
2.1
|
22.7
|
1.0
|
|
CG
|
B:ASP369
|
2.8
|
18.7
|
1.0
|
|
CG
|
B:ASP51
|
2.8
|
11.4
|
1.0
|
|
CD2
|
B:HIS370
|
3.0
|
13.3
|
1.0
|
|
OD1
|
B:ASP369
|
3.0
|
17.7
|
1.0
|
|
HD2
|
B:HIS370
|
3.1
|
13.3
|
1.0
|
|
OD2
|
B:ASP51
|
3.1
|
11.7
|
1.0
|
|
CE1
|
B:HIS370
|
3.2
|
14.0
|
1.0
|
|
HA2
|
B:GLY102
|
3.4
|
11.9
|
1.0
|
|
HA3
|
B:GLY102
|
3.5
|
11.9
|
1.0
|
|
OD1
|
B:ASP327
|
3.5
|
18.6
|
1.0
|
|
HE1
|
B:HIS370
|
3.5
|
14.0
|
1.0
|
|
P
|
B:PO4501
|
3.5
|
22.9
|
1.0
|
|
H
|
B:GLY52
|
3.5
|
10.4
|
1.0
|
|
HE1
|
B:HIS412
|
3.8
|
8.7
|
1.0
|
|
O3
|
B:PO4501
|
3.8
|
26.2
|
1.0
|
|
CA
|
B:GLY102
|
3.9
|
11.9
|
1.0
|
|
CG
|
B:ASP327
|
3.9
|
16.4
|
1.0
|
|
ZN
|
B:ZN503
|
4.0
|
15.6
|
1.0
|
|
HB2
|
B:ASP327
|
4.0
|
14.8
|
1.0
|
|
HA
|
B:ASP51
|
4.1
|
10.5
|
1.0
|
|
CB
|
B:ASP51
|
4.1
|
12.3
|
1.0
|
|
N
|
B:GLY52
|
4.1
|
10.4
|
1.0
|
|
CE1
|
B:HIS412
|
4.2
|
8.7
|
1.0
|
|
CG
|
B:HIS370
|
4.2
|
13.9
|
1.0
|
|
CB
|
B:ASP369
|
4.2
|
16.7
|
1.0
|
|
ND1
|
B:HIS370
|
4.2
|
13.7
|
1.0
|
|
N
|
B:GLY102
|
4.2
|
12.4
|
1.0
|
|
O1
|
B:PO4501
|
4.3
|
22.2
|
1.0
|
|
NE2
|
B:HIS412
|
4.3
|
6.1
|
1.0
|
|
H
|
B:GLY102
|
4.3
|
12.4
|
1.0
|
|
HB2
|
B:ASP369
|
4.4
|
16.7
|
1.0
|
|
OD2
|
B:ASP327
|
4.4
|
17.4
|
1.0
|
|
CB
|
B:ASP327
|
4.5
|
14.8
|
1.0
|
|
CA
|
B:ASP51
|
4.5
|
10.5
|
1.0
|
|
HB3
|
B:ASP327
|
4.5
|
14.8
|
1.0
|
|
O4
|
B:PO4501
|
4.5
|
21.4
|
1.0
|
|
H
|
B:HIS370
|
4.5
|
10.9
|
1.0
|
|
C
|
B:ASP51
|
4.6
|
10.2
|
1.0
|
|
HA2
|
B:GLY52
|
4.7
|
11.5
|
1.0
|
|
HG1
|
B:THR155
|
4.7
|
15.4
|
1.0
|
|
HB3
|
B:ASP369
|
4.7
|
16.7
|
1.0
|
|
HB3
|
B:ASP51
|
4.7
|
12.3
|
1.0
|
|
ZN
|
B:ZN504
|
4.8
|
13.1
|
1.0
|
|
HZ2
|
B:LYS328
|
4.8
|
19.0
|
1.0
|
|
HB2
|
B:ASP51
|
4.9
|
12.3
|
1.0
|
|
CA
|
B:GLY52
|
4.9
|
11.5
|
1.0
|
|
C
|
B:ASP101
|
4.9
|
13.8
|
1.0
|
|
HZ1
|
B:LYS328
|
5.0
|
19.0
|
1.0
|
|
ND1
|
B:HIS412
|
5.0
|
10.5
|
1.0
|
|
H
|
B:ASP369
|
5.0
|
14.8
|
1.0
|
|
Zinc binding site 5 out
of 6 in 4km4
Go back to
Zinc Binding Sites List in 4km4
Zinc binding site 5 out
of 6 in the E. Coli Alkaline Phosphatase Mutant S102G/R166S in Complex with Inorganic Phosphate
 Mono view
 Stereo pair view
|
|
A full contact list of Zinc with other atoms in the Zn binding
site number 5 of E. Coli Alkaline Phosphatase Mutant S102G/R166S in Complex with Inorganic Phosphate within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn503
b:15.6
occ:1.00
|
OD1
|
B:ASP327
|
1.9
|
18.6
|
1.0
|
|
NE2
|
B:HIS331
|
1.9
|
11.4
|
1.0
|
|
NE2
|
B:HIS412
|
2.0
|
6.1
|
1.0
|
|
O1
|
B:PO4501
|
2.3
|
22.2
|
1.0
|
|
CG
|
B:ASP327
|
2.7
|
16.4
|
1.0
|
|
OD2
|
B:ASP327
|
2.8
|
17.4
|
1.0
|
|
CD2
|
B:HIS331
|
2.9
|
12.1
|
1.0
|
|
CE1
|
B:HIS331
|
3.0
|
11.8
|
1.0
|
|
O2
|
B:PO4501
|
3.0
|
22.7
|
1.0
|
|
CE1
|
B:HIS412
|
3.0
|
8.7
|
1.0
|
|
CD2
|
B:HIS412
|
3.0
|
8.0
|
1.0
|
|
HD2
|
B:HIS331
|
3.1
|
12.1
|
1.0
|
|
HD2
|
B:HIS412
|
3.2
|
8.0
|
1.0
|
|
HE1
|
B:HIS412
|
3.2
|
8.7
|
1.0
|
|
HE1
|
B:HIS331
|
3.2
|
11.8
|
1.0
|
|
P
|
B:PO4501
|
3.3
|
22.9
|
1.0
|
|
HE1
|
B:HIS370
|
3.5
|
14.0
|
1.0
|
|
NE2
|
B:HIS372
|
3.8
|
7.6
|
1.0
|
|
HZ3
|
B:LYS328
|
4.0
|
19.0
|
1.0
|
|
CE1
|
B:HIS370
|
4.0
|
14.0
|
1.0
|
|
ZN
|
B:ZN502
|
4.0
|
10.8
|
1.0
|
|
ND1
|
B:HIS331
|
4.1
|
12.6
|
1.0
|
|
NE2
|
B:HIS370
|
4.1
|
14.2
|
1.0
|
|
CG
|
B:HIS331
|
4.1
|
13.2
|
1.0
|
|
ND1
|
B:HIS412
|
4.1
|
10.5
|
1.0
|
|
CB
|
B:ASP327
|
4.1
|
14.8
|
1.0
|
|
CG
|
B:HIS412
|
4.2
|
9.7
|
1.0
|
|
HD2
|
B:HIS372
|
4.2
|
4.8
|
1.0
|
|
O4
|
B:PO4501
|
4.2
|
21.4
|
1.0
|
|
CD2
|
B:HIS372
|
4.3
|
4.8
|
1.0
|
|
HZ2
|
B:LYS328
|
4.4
|
19.0
|
1.0
|
|
O3
|
B:PO4501
|
4.4
|
26.2
|
1.0
|
|
HB2
|
B:ASP327
|
4.4
|
14.8
|
1.0
|
|
OD1
|
B:ASP51
|
4.6
|
9.7
|
1.0
|
|
NZ
|
B:LYS328
|
4.7
|
19.0
|
1.0
|
|
HB3
|
B:ASP327
|
4.7
|
14.8
|
1.0
|
|
CE1
|
B:HIS372
|
4.7
|
7.3
|
1.0
|
|
HZ1
|
B:LYS328
|
4.8
|
19.0
|
1.0
|
|
O
|
B:ASP327
|
4.9
|
15.3
|
1.0
|
|
C
|
B:ASP327
|
5.0
|
16.0
|
1.0
|
|
HD1
|
B:HIS331
|
5.0
|
12.6
|
1.0
|
|
Zinc binding site 6 out
of 6 in 4km4
Go back to
Zinc Binding Sites List in 4km4
Zinc binding site 6 out
of 6 in the E. Coli Alkaline Phosphatase Mutant S102G/R166S in Complex with Inorganic Phosphate
 Mono view
 Stereo pair view
|
|
A full contact list of Zinc with other atoms in the Zn binding
site number 6 of E. Coli Alkaline Phosphatase Mutant S102G/R166S in Complex with Inorganic Phosphate within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn504
b:13.1
occ:1.00
|
OE2
|
B:GLU322
|
1.9
|
17.8
|
1.0
|
|
OD2
|
B:ASP51
|
1.9
|
11.7
|
1.0
|
|
OD2
|
B:ASP153
|
1.9
|
36.8
|
1.0
|
|
OG1
|
B:THR155
|
2.0
|
15.4
|
1.0
|
|
HG1
|
B:THR155
|
2.7
|
15.4
|
1.0
|
|
CD
|
B:GLU322
|
2.9
|
16.1
|
1.0
|
|
CG
|
B:ASP51
|
3.0
|
11.4
|
1.0
|
|
CG
|
B:ASP153
|
3.1
|
34.6
|
1.0
|
|
HB
|
B:THR155
|
3.1
|
14.3
|
1.0
|
|
CB
|
B:THR155
|
3.2
|
14.3
|
1.0
|
|
H
|
B:THR155
|
3.2
|
13.6
|
1.0
|
|
OE1
|
B:GLU322
|
3.2
|
16.2
|
1.0
|
|
HB2
|
B:ASP51
|
3.3
|
12.3
|
1.0
|
|
HZ1
|
B:LYS328
|
3.5
|
19.0
|
1.0
|
|
OD1
|
B:ASP153
|
3.5
|
36.0
|
1.0
|
|
CB
|
B:ASP51
|
3.7
|
12.3
|
1.0
|
|
HB1
|
B:ALA324
|
3.7
|
17.2
|
1.0
|
|
O3
|
B:PO4501
|
3.7
|
26.2
|
1.0
|
|
HA
|
B:ALA324
|
3.9
|
17.3
|
1.0
|
|
HG21
|
B:THR155
|
3.9
|
13.4
|
1.0
|
|
HZ2
|
B:LYS328
|
4.0
|
19.0
|
1.0
|
|
N
|
B:THR155
|
4.0
|
13.6
|
1.0
|
|
OD1
|
B:ASP51
|
4.1
|
9.7
|
1.0
|
|
HB3
|
B:ASP51
|
4.1
|
12.3
|
1.0
|
|
HD2
|
B:PRO156
|
4.1
|
9.3
|
1.0
|
|
HE2
|
B:LYS328
|
4.1
|
19.8
|
1.0
|
|
NZ
|
B:LYS328
|
4.1
|
19.0
|
1.0
|
|
CG2
|
B:THR155
|
4.1
|
13.4
|
1.0
|
|
CA
|
B:THR155
|
4.2
|
14.1
|
1.0
|
|
CG
|
B:GLU322
|
4.2
|
15.9
|
1.0
|
|
HG3
|
B:GLU322
|
4.3
|
15.9
|
1.0
|
|
HB2
|
B:ALA154
|
4.3
|
13.3
|
1.0
|
|
CB
|
B:ASP153
|
4.4
|
27.9
|
1.0
|
|
HB3
|
B:ALA324
|
4.4
|
17.2
|
1.0
|
|
CB
|
B:ALA324
|
4.5
|
17.2
|
1.0
|
|
HB3
|
B:ASP153
|
4.5
|
27.9
|
1.0
|
|
HG2
|
B:GLU322
|
4.6
|
15.9
|
1.0
|
|
H
|
B:ALA154
|
4.7
|
13.4
|
1.0
|
|
HB2
|
B:ALA149
|
4.7
|
15.8
|
1.0
|
|
CA
|
B:ALA324
|
4.7
|
17.3
|
1.0
|
|
HG22
|
B:THR155
|
4.7
|
13.4
|
1.0
|
|
HD3
|
B:PRO156
|
4.7
|
9.3
|
1.0
|
|
CE
|
B:LYS328
|
4.7
|
19.8
|
1.0
|
|
ZN
|
B:ZN502
|
4.8
|
10.8
|
1.0
|
|
HA
|
B:THR155
|
4.8
|
14.1
|
1.0
|
|
HB3
|
B:ALA149
|
4.8
|
15.8
|
1.0
|
|
O
|
B:ALA324
|
4.8
|
22.3
|
1.0
|
|
HG
|
B:SER147
|
4.9
|
11.7
|
1.0
|
|
HA3
|
B:GLY102
|
4.9
|
11.9
|
1.0
|
|
CD
|
B:PRO156
|
4.9
|
9.3
|
1.0
|
|
HZ3
|
B:LYS328
|
4.9
|
19.0
|
1.0
|
|
OD2
|
B:ASP369
|
5.0
|
21.5
|
1.0
|
|
N
|
B:ALA154
|
5.0
|
13.4
|
1.0
|
|
Reference:
L.D.Andrews,
T.D.Fenn,
D.Herschlag.
Ground State Destabilization By Anionic Nucleophiles Contributes to the Activity of Phosphoryl Transfer Enzymes. Plos Biol. V. 11 01599 2013.
ISSN: ISSN 1544-9173
PubMed: 23843744
DOI: 10.1371/JOURNAL.PBIO.1001599
Page generated: Wed Dec 16 05:29:24 2020
|
