Potassium in PDB 9gku: Crystal Structure of Propanil Hydrolase (Prph) From Sphingomonas Sp. Y57
Protein crystallography data
The structure of Crystal Structure of Propanil Hydrolase (Prph) From Sphingomonas Sp. Y57, PDB code: 9gku
was solved by
L.G.Graf,
L.Lammers,
G.J.Palm,
S.Schulze,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
|
Resolution Low / High (Å)
|
44.56 /
1.48
|
|
Space group
|
P 1
|
|
Cell size a, b, c (Å), α, β, γ (°)
|
103.861,
103.698,
104.499,
113.6,
93,
120.61
|
|
R / Rfree (%)
|
17.3 /
19.9
|
Other elements in 9gku:
The structure of Crystal Structure of Propanil Hydrolase (Prph) From Sphingomonas Sp. Y57 also contains other interesting chemical elements:
Potassium Binding Sites:
The binding sites of Potassium atom in the Crystal Structure of Propanil Hydrolase (Prph) From Sphingomonas Sp. Y57
(pdb code 9gku). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total 8 binding sites of Potassium where determined in the
Crystal Structure of Propanil Hydrolase (Prph) From Sphingomonas Sp. Y57, PDB code: 9gku:
Jump to Potassium binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Potassium binding site 1 out
of 8 in 9gku
Go back to
Potassium Binding Sites List in 9gku
Potassium binding site 1 out
of 8 in the Crystal Structure of Propanil Hydrolase (Prph) From Sphingomonas Sp. Y57
 Mono view
 Stereo pair view
|
|
A full contact list of Potassium with other atoms in the K binding
site number 1 of Crystal Structure of Propanil Hydrolase (Prph) From Sphingomonas Sp. Y57 within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K404
b:23.3
occ:1.00
|
O
|
A:ASP190
|
2.5
|
19.3
|
1.0
|
|
O
|
A:VAL212
|
2.6
|
21.1
|
1.0
|
|
O
|
A:HIS192
|
2.7
|
21.7
|
1.0
|
|
OD1
|
A:ASP188
|
2.7
|
22.1
|
1.0
|
|
OG
|
A:SER211
|
2.8
|
24.1
|
1.0
|
|
O
|
A:ASP188
|
2.9
|
20.4
|
1.0
|
|
CG
|
A:ASP188
|
3.2
|
22.8
|
1.0
|
|
C
|
A:VAL212
|
3.6
|
21.3
|
1.0
|
|
C
|
A:ASP188
|
3.6
|
21.1
|
1.0
|
|
C
|
A:ASP190
|
3.6
|
20.1
|
1.0
|
|
C
|
A:HIS192
|
3.7
|
19.4
|
1.0
|
|
N
|
A:VAL212
|
3.8
|
21.2
|
1.0
|
|
CB
|
A:ASP188
|
3.8
|
21.9
|
1.0
|
|
OD2
|
A:ASP188
|
3.9
|
24.7
|
1.0
|
|
CB
|
A:SER211
|
3.9
|
23.0
|
1.0
|
|
CB
|
A:HIS213
|
3.9
|
19.1
|
1.0
|
|
N
|
A:ASP190
|
4.0
|
20.9
|
1.0
|
|
CA
|
A:SER211
|
4.1
|
21.7
|
1.0
|
|
CA
|
A:ASP190
|
4.2
|
20.3
|
1.0
|
|
C
|
A:SER211
|
4.2
|
22.1
|
1.0
|
|
N
|
A:GLY194
|
4.3
|
22.2
|
1.0
|
|
N
|
A:TRP189
|
4.3
|
20.8
|
1.0
|
|
C
|
A:TRP189
|
4.3
|
20.7
|
1.0
|
|
CA
|
A:ASP188
|
4.3
|
21.4
|
1.0
|
|
N
|
A:HIS192
|
4.3
|
21.1
|
1.0
|
|
CA
|
A:VAL212
|
4.3
|
21.8
|
1.0
|
|
CA
|
A:HIS213
|
4.4
|
21.4
|
1.0
|
|
CA
|
A:HIS193
|
4.4
|
19.7
|
1.0
|
|
N
|
A:HIS213
|
4.4
|
20.7
|
1.0
|
|
CB
|
A:ASP190
|
4.4
|
20.4
|
1.0
|
|
CA
|
A:TRP189
|
4.4
|
21.7
|
1.0
|
|
N
|
A:HIS193
|
4.5
|
20.4
|
1.0
|
|
ND1
|
A:HIS213
|
4.5
|
23.2
|
1.0
|
|
C
|
A:VAL191
|
4.6
|
20.9
|
1.0
|
|
O
|
A:HOH572
|
4.6
|
22.0
|
1.0
|
|
C
|
A:HIS193
|
4.6
|
21.9
|
1.0
|
|
N
|
A:VAL191
|
4.7
|
19.6
|
1.0
|
|
CG
|
A:HIS213
|
4.7
|
20.9
|
1.0
|
|
CA
|
A:HIS192
|
4.7
|
19.4
|
1.0
|
|
CE1
|
A:HIS152
|
4.7
|
23.5
|
1.0
|
|
ND1
|
A:HIS152
|
4.9
|
21.7
|
1.0
|
|
CA
|
A:VAL191
|
4.9
|
18.6
|
1.0
|
|
O
|
A:TRP189
|
5.0
|
20.8
|
1.0
|
|
Potassium binding site 2 out
of 8 in 9gku
Go back to
Potassium Binding Sites List in 9gku
Potassium binding site 2 out
of 8 in the Crystal Structure of Propanil Hydrolase (Prph) From Sphingomonas Sp. Y57
 Mono view
 Stereo pair view
|
|
A full contact list of Potassium with other atoms in the K binding
site number 2 of Crystal Structure of Propanil Hydrolase (Prph) From Sphingomonas Sp. Y57 within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:K404
b:23.5
occ:0.76
|
O
|
B:ASP190
|
2.5
|
22.9
|
1.0
|
|
O
|
B:VAL212
|
2.6
|
24.7
|
1.0
|
|
O
|
B:HIS192
|
2.7
|
24.4
|
1.0
|
|
OD1
|
B:ASP188
|
2.7
|
28.3
|
1.0
|
|
OG
|
B:SER211
|
2.9
|
27.1
|
1.0
|
|
O
|
B:ASP188
|
3.0
|
25.2
|
1.0
|
|
CG
|
B:ASP188
|
3.2
|
25.1
|
1.0
|
|
C
|
B:ASP190
|
3.6
|
22.9
|
1.0
|
|
C
|
B:VAL212
|
3.6
|
24.8
|
1.0
|
|
C
|
B:ASP188
|
3.6
|
26.2
|
1.0
|
|
C
|
B:HIS192
|
3.7
|
23.5
|
1.0
|
|
CB
|
B:ASP188
|
3.8
|
25.2
|
1.0
|
|
N
|
B:VAL212
|
3.8
|
24.6
|
1.0
|
|
OD2
|
B:ASP188
|
3.9
|
27.5
|
1.0
|
|
CB
|
B:HIS213
|
3.9
|
22.8
|
1.0
|
|
N
|
B:ASP190
|
4.0
|
20.9
|
1.0
|
|
CB
|
B:SER211
|
4.0
|
27.1
|
1.0
|
|
CA
|
B:ASP190
|
4.2
|
20.7
|
1.0
|
|
CA
|
B:SER211
|
4.2
|
25.6
|
1.0
|
|
N
|
B:GLY194
|
4.2
|
22.9
|
1.0
|
|
N
|
B:TRP189
|
4.3
|
24.3
|
1.0
|
|
C
|
B:TRP189
|
4.3
|
21.1
|
1.0
|
|
CB
|
B:ASP190
|
4.3
|
21.0
|
1.0
|
|
C
|
B:SER211
|
4.3
|
25.4
|
1.0
|
|
CA
|
B:ASP188
|
4.3
|
25.4
|
1.0
|
|
N
|
B:HIS192
|
4.3
|
22.9
|
1.0
|
|
CA
|
B:HIS193
|
4.3
|
25.1
|
1.0
|
|
CA
|
B:HIS213
|
4.3
|
21.6
|
1.0
|
|
N
|
B:HIS213
|
4.4
|
23.5
|
1.0
|
|
CA
|
B:VAL212
|
4.4
|
22.4
|
1.0
|
|
CA
|
B:TRP189
|
4.4
|
21.3
|
1.0
|
|
N
|
B:HIS193
|
4.5
|
23.6
|
1.0
|
|
ND1
|
B:HIS213
|
4.5
|
25.5
|
1.0
|
|
C
|
B:VAL191
|
4.6
|
21.3
|
1.0
|
|
O
|
B:HOH566
|
4.6
|
23.7
|
1.0
|
|
N
|
B:VAL191
|
4.6
|
21.4
|
1.0
|
|
C
|
B:HIS193
|
4.6
|
22.7
|
1.0
|
|
CA
|
B:HIS192
|
4.7
|
23.4
|
1.0
|
|
CG
|
B:HIS213
|
4.7
|
23.3
|
1.0
|
|
CE1
|
B:HIS152
|
4.7
|
27.1
|
1.0
|
|
ND1
|
B:HIS152
|
4.9
|
24.9
|
1.0
|
|
CA
|
B:VAL191
|
4.9
|
22.1
|
1.0
|
|
O
|
B:TRP189
|
5.0
|
23.5
|
1.0
|
|
Potassium binding site 3 out
of 8 in 9gku
Go back to
Potassium Binding Sites List in 9gku
Potassium binding site 3 out
of 8 in the Crystal Structure of Propanil Hydrolase (Prph) From Sphingomonas Sp. Y57
 Mono view
 Stereo pair view
|
|
A full contact list of Potassium with other atoms in the K binding
site number 3 of Crystal Structure of Propanil Hydrolase (Prph) From Sphingomonas Sp. Y57 within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:K405
b:21.4
occ:0.87
|
O
|
C:ASP190
|
2.5
|
20.3
|
1.0
|
|
O
|
C:VAL212
|
2.6
|
21.1
|
1.0
|
|
OD1
|
C:ASP188
|
2.7
|
23.4
|
1.0
|
|
O
|
C:HIS192
|
2.7
|
21.9
|
1.0
|
|
OG
|
C:SER211
|
2.8
|
23.6
|
1.0
|
|
O
|
C:ASP188
|
2.9
|
22.0
|
1.0
|
|
CG
|
C:ASP188
|
3.2
|
24.5
|
1.0
|
|
C
|
C:ASP188
|
3.6
|
19.7
|
1.0
|
|
C
|
C:VAL212
|
3.6
|
22.6
|
1.0
|
|
C
|
C:ASP190
|
3.6
|
20.5
|
1.0
|
|
N
|
C:VAL212
|
3.7
|
21.6
|
1.0
|
|
C
|
C:HIS192
|
3.8
|
19.4
|
1.0
|
|
CB
|
C:ASP188
|
3.8
|
20.9
|
1.0
|
|
OD2
|
C:ASP188
|
3.9
|
25.9
|
1.0
|
|
CB
|
C:SER211
|
3.9
|
23.3
|
1.0
|
|
CB
|
C:HIS213
|
4.0
|
20.4
|
1.0
|
|
N
|
C:ASP190
|
4.0
|
22.1
|
1.0
|
|
CA
|
C:SER211
|
4.1
|
21.5
|
1.0
|
|
CA
|
C:ASP190
|
4.2
|
19.3
|
1.0
|
|
N
|
C:TRP189
|
4.2
|
21.6
|
1.0
|
|
C
|
C:SER211
|
4.2
|
21.9
|
1.0
|
|
C
|
C:TRP189
|
4.3
|
22.9
|
1.0
|
|
N
|
C:GLY194
|
4.3
|
22.1
|
1.0
|
|
CA
|
C:ASP188
|
4.3
|
21.1
|
1.0
|
|
CA
|
C:VAL212
|
4.3
|
21.8
|
1.0
|
|
N
|
C:HIS192
|
4.4
|
20.1
|
1.0
|
|
N
|
C:HIS213
|
4.4
|
21.7
|
1.0
|
|
CA
|
C:HIS213
|
4.4
|
20.2
|
1.0
|
|
CB
|
C:ASP190
|
4.4
|
21.9
|
1.0
|
|
CA
|
C:TRP189
|
4.4
|
21.8
|
1.0
|
|
CA
|
C:HIS193
|
4.4
|
20.1
|
1.0
|
|
ND1
|
C:HIS213
|
4.4
|
22.9
|
1.0
|
|
N
|
C:HIS193
|
4.5
|
21.0
|
1.0
|
|
O
|
C:HOH589
|
4.6
|
22.0
|
1.0
|
|
C
|
C:VAL191
|
4.6
|
21.1
|
1.0
|
|
C
|
C:HIS193
|
4.7
|
19.8
|
1.0
|
|
N
|
C:VAL191
|
4.7
|
19.2
|
1.0
|
|
CG
|
C:HIS213
|
4.7
|
22.8
|
1.0
|
|
CE1
|
C:HIS152
|
4.7
|
22.9
|
1.0
|
|
CA
|
C:HIS192
|
4.7
|
19.8
|
1.0
|
|
ND1
|
C:HIS152
|
4.9
|
22.3
|
1.0
|
|
CA
|
C:VAL191
|
5.0
|
19.6
|
1.0
|
|
O
|
C:TRP189
|
5.0
|
22.2
|
1.0
|
|
Potassium binding site 4 out
of 8 in 9gku
Go back to
Potassium Binding Sites List in 9gku
Potassium binding site 4 out
of 8 in the Crystal Structure of Propanil Hydrolase (Prph) From Sphingomonas Sp. Y57
 Mono view
 Stereo pair view
|
|
A full contact list of Potassium with other atoms in the K binding
site number 4 of Crystal Structure of Propanil Hydrolase (Prph) From Sphingomonas Sp. Y57 within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:K403
b:21.6
occ:0.73
|
O
|
D:ASP190
|
2.5
|
21.1
|
1.0
|
|
O
|
D:VAL212
|
2.6
|
23.1
|
1.0
|
|
O
|
D:HIS192
|
2.7
|
22.2
|
1.0
|
|
OD1
|
D:ASP188
|
2.7
|
24.1
|
1.0
|
|
OG
|
D:SER211
|
2.8
|
23.8
|
1.0
|
|
O
|
D:ASP188
|
2.9
|
23.5
|
1.0
|
|
CG
|
D:ASP188
|
3.2
|
23.5
|
1.0
|
|
C
|
D:VAL212
|
3.6
|
20.8
|
1.0
|
|
C
|
D:ASP190
|
3.6
|
21.7
|
1.0
|
|
C
|
D:ASP188
|
3.6
|
21.8
|
1.0
|
|
C
|
D:HIS192
|
3.7
|
21.7
|
1.0
|
|
N
|
D:VAL212
|
3.8
|
22.1
|
1.0
|
|
CB
|
D:ASP188
|
3.8
|
22.2
|
1.0
|
|
OD2
|
D:ASP188
|
3.8
|
24.7
|
1.0
|
|
CB
|
D:HIS213
|
3.9
|
19.8
|
1.0
|
|
CB
|
D:SER211
|
4.0
|
22.9
|
1.0
|
|
N
|
D:ASP190
|
4.0
|
20.3
|
1.0
|
|
CA
|
D:SER211
|
4.2
|
22.6
|
1.0
|
|
CA
|
D:ASP190
|
4.2
|
19.1
|
1.0
|
|
N
|
D:GLY194
|
4.2
|
22.0
|
1.0
|
|
N
|
D:TRP189
|
4.3
|
20.4
|
1.0
|
|
C
|
D:TRP189
|
4.3
|
20.8
|
1.0
|
|
C
|
D:SER211
|
4.3
|
23.8
|
1.0
|
|
CA
|
D:ASP188
|
4.3
|
21.1
|
1.0
|
|
N
|
D:HIS192
|
4.3
|
19.7
|
1.0
|
|
CB
|
D:ASP190
|
4.3
|
20.1
|
1.0
|
|
CA
|
D:VAL212
|
4.3
|
20.3
|
1.0
|
|
CA
|
D:HIS193
|
4.3
|
22.3
|
1.0
|
|
CA
|
D:HIS213
|
4.3
|
19.3
|
1.0
|
|
N
|
D:HIS213
|
4.4
|
20.0
|
1.0
|
|
CA
|
D:TRP189
|
4.4
|
19.7
|
1.0
|
|
ND1
|
D:HIS213
|
4.5
|
24.1
|
1.0
|
|
N
|
D:HIS193
|
4.5
|
22.4
|
1.0
|
|
O
|
D:HOH559
|
4.6
|
21.1
|
1.0
|
|
C
|
D:HIS193
|
4.6
|
21.5
|
1.0
|
|
C
|
D:VAL191
|
4.6
|
21.1
|
1.0
|
|
N
|
D:VAL191
|
4.6
|
19.5
|
1.0
|
|
CA
|
D:HIS192
|
4.7
|
20.9
|
1.0
|
|
CG
|
D:HIS213
|
4.7
|
20.6
|
1.0
|
|
CE1
|
D:HIS152
|
4.7
|
24.4
|
1.0
|
|
ND1
|
D:HIS152
|
4.9
|
22.4
|
1.0
|
|
CA
|
D:VAL191
|
4.9
|
20.7
|
1.0
|
|
O
|
D:TRP189
|
5.0
|
21.5
|
1.0
|
|
Potassium binding site 5 out
of 8 in 9gku
Go back to
Potassium Binding Sites List in 9gku
Potassium binding site 5 out
of 8 in the Crystal Structure of Propanil Hydrolase (Prph) From Sphingomonas Sp. Y57
 Mono view
 Stereo pair view
|
|
A full contact list of Potassium with other atoms in the K binding
site number 5 of Crystal Structure of Propanil Hydrolase (Prph) From Sphingomonas Sp. Y57 within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:K405
b:21.0
occ:1.00
|
O
|
E:ASP190
|
2.5
|
18.2
|
1.0
|
|
O
|
E:VAL212
|
2.7
|
19.5
|
1.0
|
|
O
|
E:HIS192
|
2.7
|
18.8
|
1.0
|
|
OD1
|
E:ASP188
|
2.8
|
20.0
|
1.0
|
|
OG
|
E:SER211
|
2.8
|
20.6
|
1.0
|
|
O
|
E:ASP188
|
2.9
|
18.6
|
1.0
|
|
CG
|
E:ASP188
|
3.2
|
22.6
|
1.0
|
|
C
|
E:ASP190
|
3.6
|
16.2
|
1.0
|
|
C
|
E:VAL212
|
3.6
|
19.3
|
1.0
|
|
C
|
E:ASP188
|
3.6
|
19.1
|
1.0
|
|
C
|
E:HIS192
|
3.7
|
19.6
|
1.0
|
|
N
|
E:VAL212
|
3.8
|
18.7
|
1.0
|
|
CB
|
E:ASP188
|
3.8
|
20.0
|
1.0
|
|
OD2
|
E:ASP188
|
3.9
|
22.9
|
1.0
|
|
CB
|
E:SER211
|
3.9
|
19.6
|
1.0
|
|
CB
|
E:HIS213
|
4.0
|
17.0
|
1.0
|
|
N
|
E:ASP190
|
4.0
|
19.4
|
1.0
|
|
CA
|
E:SER211
|
4.1
|
16.9
|
1.0
|
|
CA
|
E:ASP190
|
4.2
|
18.0
|
1.0
|
|
N
|
E:GLY194
|
4.2
|
19.8
|
1.0
|
|
C
|
E:SER211
|
4.3
|
19.7
|
1.0
|
|
CB
|
E:ASP190
|
4.3
|
18.6
|
1.0
|
|
N
|
E:TRP189
|
4.3
|
19.9
|
1.0
|
|
C
|
E:TRP189
|
4.3
|
20.2
|
1.0
|
|
CA
|
E:HIS193
|
4.3
|
18.2
|
1.0
|
|
CA
|
E:ASP188
|
4.3
|
19.3
|
1.0
|
|
N
|
E:HIS192
|
4.4
|
18.8
|
1.0
|
|
CA
|
E:HIS213
|
4.4
|
16.9
|
1.0
|
|
CA
|
E:VAL212
|
4.4
|
17.6
|
1.0
|
|
N
|
E:HIS213
|
4.4
|
16.8
|
1.0
|
|
CA
|
E:TRP189
|
4.4
|
19.5
|
1.0
|
|
N
|
E:HIS193
|
4.5
|
18.6
|
1.0
|
|
ND1
|
E:HIS213
|
4.5
|
20.3
|
1.0
|
|
C
|
E:HIS193
|
4.6
|
19.8
|
1.0
|
|
O
|
E:HOH614
|
4.6
|
20.4
|
1.0
|
|
C
|
E:VAL191
|
4.6
|
19.9
|
1.0
|
|
N
|
E:VAL191
|
4.7
|
17.9
|
1.0
|
|
CG
|
E:HIS213
|
4.7
|
18.3
|
1.0
|
|
CA
|
E:HIS192
|
4.7
|
17.9
|
1.0
|
|
CE1
|
E:HIS152
|
4.7
|
19.7
|
1.0
|
|
ND1
|
E:HIS152
|
4.9
|
20.9
|
1.0
|
|
CA
|
E:VAL191
|
5.0
|
17.4
|
1.0
|
|
Potassium binding site 6 out
of 8 in 9gku
Go back to
Potassium Binding Sites List in 9gku
Potassium binding site 6 out
of 8 in the Crystal Structure of Propanil Hydrolase (Prph) From Sphingomonas Sp. Y57
 Mono view
 Stereo pair view
|
|
A full contact list of Potassium with other atoms in the K binding
site number 6 of Crystal Structure of Propanil Hydrolase (Prph) From Sphingomonas Sp. Y57 within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:K404
b:21.1
occ:1.00
|
O
|
F:ASP190
|
2.5
|
18.5
|
1.0
|
|
O
|
F:VAL212
|
2.6
|
20.7
|
1.0
|
|
O
|
F:HIS192
|
2.7
|
19.7
|
1.0
|
|
OD1
|
F:ASP188
|
2.8
|
20.9
|
1.0
|
|
OG
|
F:SER211
|
2.8
|
19.9
|
1.0
|
|
O
|
F:ASP188
|
2.9
|
18.7
|
1.0
|
|
CG
|
F:ASP188
|
3.2
|
20.4
|
1.0
|
|
C
|
F:VAL212
|
3.6
|
18.3
|
1.0
|
|
C
|
F:ASP188
|
3.6
|
19.4
|
1.0
|
|
C
|
F:ASP190
|
3.6
|
17.9
|
1.0
|
|
C
|
F:HIS192
|
3.7
|
18.9
|
1.0
|
|
N
|
F:VAL212
|
3.8
|
18.1
|
1.0
|
|
CB
|
F:ASP188
|
3.8
|
20.4
|
1.0
|
|
OD2
|
F:ASP188
|
3.9
|
21.3
|
1.0
|
|
CB
|
F:HIS213
|
3.9
|
17.7
|
1.0
|
|
CB
|
F:SER211
|
3.9
|
20.6
|
1.0
|
|
N
|
F:ASP190
|
4.0
|
19.3
|
1.0
|
|
CA
|
F:SER211
|
4.1
|
18.8
|
1.0
|
|
CA
|
F:ASP190
|
4.2
|
18.6
|
1.0
|
|
C
|
F:SER211
|
4.3
|
20.2
|
1.0
|
|
N
|
F:TRP189
|
4.3
|
19.2
|
1.0
|
|
N
|
F:GLY194
|
4.3
|
19.3
|
1.0
|
|
C
|
F:TRP189
|
4.3
|
19.9
|
1.0
|
|
CA
|
F:ASP188
|
4.3
|
18.6
|
1.0
|
|
CB
|
F:ASP190
|
4.3
|
18.2
|
1.0
|
|
CA
|
F:HIS193
|
4.3
|
17.5
|
1.0
|
|
CA
|
F:HIS213
|
4.3
|
17.8
|
1.0
|
|
CA
|
F:VAL212
|
4.4
|
17.4
|
1.0
|
|
N
|
F:HIS192
|
4.4
|
17.0
|
1.0
|
|
N
|
F:HIS213
|
4.4
|
17.0
|
1.0
|
|
CA
|
F:TRP189
|
4.4
|
19.7
|
1.0
|
|
N
|
F:HIS193
|
4.5
|
19.0
|
1.0
|
|
ND1
|
F:HIS213
|
4.5
|
20.8
|
1.0
|
|
O
|
F:HOH652
|
4.6
|
20.3
|
1.0
|
|
C
|
F:HIS193
|
4.6
|
18.3
|
1.0
|
|
C
|
F:VAL191
|
4.6
|
18.8
|
1.0
|
|
N
|
F:VAL191
|
4.7
|
18.7
|
1.0
|
|
CG
|
F:HIS213
|
4.7
|
19.1
|
1.0
|
|
CA
|
F:HIS192
|
4.7
|
17.9
|
1.0
|
|
CE1
|
F:HIS152
|
4.8
|
20.3
|
1.0
|
|
ND1
|
F:HIS152
|
4.9
|
19.3
|
1.0
|
|
CA
|
F:VAL191
|
5.0
|
18.2
|
1.0
|
|
Potassium binding site 7 out
of 8 in 9gku
Go back to
Potassium Binding Sites List in 9gku
Potassium binding site 7 out
of 8 in the Crystal Structure of Propanil Hydrolase (Prph) From Sphingomonas Sp. Y57
 Mono view
 Stereo pair view
|
|
A full contact list of Potassium with other atoms in the K binding
site number 7 of Crystal Structure of Propanil Hydrolase (Prph) From Sphingomonas Sp. Y57 within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:K404
b:25.8
occ:0.68
|
O
|
G:ASP190
|
2.5
|
23.1
|
1.0
|
|
O
|
G:VAL212
|
2.7
|
23.5
|
1.0
|
|
O
|
G:HIS192
|
2.7
|
25.8
|
1.0
|
|
OD1
|
G:ASP188
|
2.7
|
26.3
|
1.0
|
|
OG
|
G:SER211
|
2.8
|
23.3
|
1.0
|
|
O
|
G:ASP188
|
3.1
|
20.9
|
1.0
|
|
CG
|
G:ASP188
|
3.2
|
23.2
|
1.0
|
|
C
|
G:VAL212
|
3.6
|
22.1
|
1.0
|
|
C
|
G:ASP190
|
3.6
|
22.8
|
1.0
|
|
C
|
G:ASP188
|
3.6
|
20.4
|
1.0
|
|
CB
|
G:ASP188
|
3.7
|
21.2
|
1.0
|
|
N
|
G:VAL212
|
3.8
|
20.6
|
1.0
|
|
C
|
G:HIS192
|
3.8
|
23.6
|
1.0
|
|
OD2
|
G:ASP188
|
3.8
|
25.6
|
1.0
|
|
CB
|
G:HIS213
|
3.8
|
21.0
|
1.0
|
|
CB
|
G:SER211
|
3.9
|
22.3
|
1.0
|
|
N
|
G:ASP190
|
3.9
|
21.1
|
1.0
|
|
CA
|
G:SER211
|
4.1
|
19.8
|
1.0
|
|
N
|
G:GLY194
|
4.2
|
22.4
|
1.0
|
|
CA
|
G:ASP190
|
4.2
|
20.4
|
1.0
|
|
C
|
G:SER211
|
4.2
|
21.7
|
1.0
|
|
N
|
G:TRP189
|
4.3
|
20.4
|
1.0
|
|
C
|
G:TRP189
|
4.3
|
19.0
|
1.0
|
|
CA
|
G:HIS213
|
4.3
|
18.0
|
1.0
|
|
CA
|
G:HIS193
|
4.3
|
20.8
|
1.0
|
|
CA
|
G:ASP188
|
4.3
|
21.0
|
1.0
|
|
N
|
G:HIS213
|
4.3
|
20.0
|
1.0
|
|
CA
|
G:VAL212
|
4.3
|
19.0
|
1.0
|
|
CB
|
G:ASP190
|
4.3
|
20.4
|
1.0
|
|
N
|
G:HIS192
|
4.4
|
21.7
|
1.0
|
|
CA
|
G:TRP189
|
4.4
|
18.8
|
1.0
|
|
N
|
G:HIS193
|
4.5
|
20.8
|
1.0
|
|
ND1
|
G:HIS213
|
4.5
|
22.8
|
1.0
|
|
C
|
G:HIS193
|
4.6
|
20.0
|
1.0
|
|
C
|
G:VAL191
|
4.7
|
21.9
|
1.0
|
|
CG
|
G:HIS213
|
4.7
|
22.2
|
1.0
|
|
N
|
G:VAL191
|
4.7
|
20.4
|
1.0
|
|
O
|
G:HOH563
|
4.7
|
21.7
|
1.0
|
|
CA
|
G:HIS192
|
4.8
|
22.7
|
1.0
|
|
CE1
|
G:HIS152
|
4.8
|
24.3
|
1.0
|
|
ND1
|
G:HIS152
|
4.9
|
23.8
|
1.0
|
|
CA
|
G:VAL191
|
5.0
|
21.4
|
1.0
|
|
O
|
G:TRP189
|
5.0
|
22.3
|
1.0
|
|
Potassium binding site 8 out
of 8 in 9gku
Go back to
Potassium Binding Sites List in 9gku
Potassium binding site 8 out
of 8 in the Crystal Structure of Propanil Hydrolase (Prph) From Sphingomonas Sp. Y57
 Mono view
 Stereo pair view
|
|
A full contact list of Potassium with other atoms in the K binding
site number 8 of Crystal Structure of Propanil Hydrolase (Prph) From Sphingomonas Sp. Y57 within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
H:K404
b:27.5
occ:0.57
|
O
|
H:ASP190
|
2.5
|
24.8
|
1.0
|
|
O
|
H:VAL212
|
2.7
|
24.7
|
1.0
|
|
O
|
H:HIS192
|
2.8
|
27.3
|
1.0
|
|
OG
|
H:SER211
|
2.8
|
24.7
|
1.0
|
|
OD2
|
H:ASP188
|
2.8
|
28.2
|
1.0
|
|
O
|
H:ASP188
|
3.1
|
23.5
|
1.0
|
|
CG
|
H:ASP188
|
3.3
|
27.3
|
1.0
|
|
C
|
H:VAL212
|
3.5
|
22.9
|
1.0
|
|
C
|
H:ASP190
|
3.6
|
23.9
|
1.0
|
|
C
|
H:ASP188
|
3.7
|
23.8
|
1.0
|
|
N
|
H:VAL212
|
3.7
|
21.9
|
1.0
|
|
C
|
H:HIS192
|
3.8
|
28.0
|
1.0
|
|
CB
|
H:ASP188
|
3.8
|
24.4
|
1.0
|
|
CB
|
H:HIS213
|
3.8
|
21.5
|
1.0
|
|
CB
|
H:SER211
|
3.9
|
25.9
|
1.0
|
|
OD1
|
H:ASP188
|
3.9
|
29.0
|
1.0
|
|
N
|
H:ASP190
|
4.0
|
23.0
|
1.0
|
|
CA
|
H:SER211
|
4.1
|
22.9
|
1.0
|
|
N
|
H:GLY194
|
4.2
|
23.9
|
1.0
|
|
CA
|
H:ASP190
|
4.2
|
23.1
|
1.0
|
|
CA
|
H:HIS213
|
4.2
|
20.6
|
1.0
|
|
C
|
H:SER211
|
4.2
|
24.3
|
1.0
|
|
N
|
H:HIS213
|
4.3
|
21.7
|
1.0
|
|
CA
|
H:HIS193
|
4.3
|
22.8
|
1.0
|
|
C
|
H:TRP189
|
4.3
|
20.6
|
1.0
|
|
N
|
H:TRP189
|
4.3
|
23.7
|
1.0
|
|
CA
|
H:VAL212
|
4.3
|
22.6
|
1.0
|
|
CA
|
H:ASP188
|
4.4
|
23.6
|
1.0
|
|
CB
|
H:ASP190
|
4.4
|
23.8
|
1.0
|
|
N
|
H:HIS192
|
4.4
|
21.8
|
1.0
|
|
CA
|
H:TRP189
|
4.4
|
21.7
|
1.0
|
|
N
|
H:HIS193
|
4.5
|
21.9
|
1.0
|
|
ND1
|
H:HIS213
|
4.5
|
26.8
|
1.0
|
|
C
|
H:HIS193
|
4.6
|
23.1
|
1.0
|
|
CG
|
H:HIS213
|
4.6
|
23.2
|
1.0
|
|
C
|
H:VAL191
|
4.6
|
22.8
|
1.0
|
|
N
|
H:VAL191
|
4.6
|
22.5
|
1.0
|
|
O
|
H:HOH559
|
4.7
|
23.6
|
1.0
|
|
CA
|
H:HIS192
|
4.7
|
24.4
|
1.0
|
|
CE1
|
H:HIS152
|
4.8
|
26.9
|
1.0
|
|
CA
|
H:VAL191
|
4.9
|
23.7
|
1.0
|
|
ND1
|
H:HIS152
|
4.9
|
26.9
|
1.0
|
|
O
|
H:TRP189
|
5.0
|
24.0
|
1.0
|
|
Reference:
L.G.Graf,
C.Moreno-Yruela,
C.Qin,
S.Schulze,
G.J.Palm,
O.Schmoeker,
N.Wang,
D.Hocking,
L.Jebeli,
B.Girbardt,
L.Berndt,
D.M.Weis,
M.Janetzky,
D.Zuehlke,
S.Sievers,
R.A.Strugnell,
C.A.Olsen,
K.Hofmann,
M.Lammers.
Distribution and Diversity of Classical Deacylases in Bacteria Nature Communications 2024.
Page generated: Sat Aug 9 19:06:05 2025
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