Potassium in PDB 1ynf: Crystal Structure of N-Succinylarginine Dihydrolase, Astb, Bound to Substrate and Product, An Enzyme From the Arginine Catabolic Pathway of Escherichia Coli
Protein crystallography data
The structure of Crystal Structure of N-Succinylarginine Dihydrolase, Astb, Bound to Substrate and Product, An Enzyme From the Arginine Catabolic Pathway of Escherichia Coli, PDB code: 1ynf
was solved by
A.Tocilj,
J.D.Schrag,
Y.Li,
B.L.Schneider,
L.Reitzer,
A.Matte,
M.Cygler,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
27.32 /
1.90
|
Space group
|
P 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
55.834,
94.172,
139.660,
75.41,
78.38,
89.74
|
R / Rfree (%)
|
21.4 /
25.2
|
Potassium Binding Sites:
The binding sites of Potassium atom in the Crystal Structure of N-Succinylarginine Dihydrolase, Astb, Bound to Substrate and Product, An Enzyme From the Arginine Catabolic Pathway of Escherichia Coli
(pdb code 1ynf). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total 6 binding sites of Potassium where determined in the
Crystal Structure of N-Succinylarginine Dihydrolase, Astb, Bound to Substrate and Product, An Enzyme From the Arginine Catabolic Pathway of Escherichia Coli, PDB code: 1ynf:
Jump to Potassium binding site number:
1;
2;
3;
4;
5;
6;
Potassium binding site 1 out
of 6 in 1ynf
Go back to
Potassium Binding Sites List in 1ynf
Potassium binding site 1 out
of 6 in the Crystal Structure of N-Succinylarginine Dihydrolase, Astb, Bound to Substrate and Product, An Enzyme From the Arginine Catabolic Pathway of Escherichia Coli
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 N-Succinylarginine Dihydrolase, Astb, Bound to Substrate and Product, An Enzyme From the Arginine Catabolic Pathway of Escherichia Coli within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K448
b:24.0
occ:1.00
|
O
|
A:ILE345
|
2.6
|
24.1
|
1.0
|
OD1
|
A:ASN343
|
2.7
|
21.6
|
1.0
|
O
|
A:LEU339
|
2.8
|
26.7
|
1.0
|
O
|
A:ALA341
|
2.8
|
27.6
|
1.0
|
O
|
A:HOH620
|
2.9
|
24.2
|
1.0
|
O
|
A:ASN343
|
3.0
|
23.8
|
1.0
|
O
|
A:LEU338
|
3.3
|
24.8
|
1.0
|
CG
|
A:ASN343
|
3.4
|
19.4
|
1.0
|
C
|
A:LEU339
|
3.5
|
26.6
|
1.0
|
C
|
A:ILE345
|
3.6
|
23.0
|
1.0
|
ND2
|
A:ASN343
|
3.8
|
16.9
|
1.0
|
C
|
A:ASN343
|
3.8
|
24.2
|
1.0
|
N
|
A:ASN343
|
3.9
|
26.5
|
1.0
|
C
|
A:ALA341
|
3.9
|
28.3
|
1.0
|
CA
|
A:LEU339
|
4.0
|
25.6
|
1.0
|
N
|
A:ILE345
|
4.1
|
23.6
|
1.0
|
N
|
A:ALA341
|
4.2
|
27.2
|
1.0
|
CA
|
A:ASN343
|
4.3
|
24.9
|
1.0
|
CA
|
A:ILE345
|
4.3
|
22.9
|
1.0
|
N
|
A:ALA340
|
4.3
|
25.9
|
1.0
|
C
|
A:LEU338
|
4.4
|
26.0
|
1.0
|
CB
|
A:ASN343
|
4.4
|
22.3
|
1.0
|
C
|
A:ALA340
|
4.5
|
28.2
|
1.0
|
CB
|
A:ILE345
|
4.6
|
20.9
|
1.0
|
N
|
A:SER346
|
4.6
|
23.7
|
1.0
|
CA
|
A:ALA341
|
4.7
|
27.9
|
1.0
|
C
|
A:PRO344
|
4.7
|
23.2
|
1.0
|
N
|
A:LEU339
|
4.7
|
24.4
|
1.0
|
CA
|
A:ALA340
|
4.7
|
27.4
|
1.0
|
O
|
A:HOH664
|
4.8
|
41.4
|
1.0
|
N
|
A:PRO344
|
4.8
|
23.4
|
1.0
|
CA
|
A:SER346
|
4.9
|
24.5
|
1.0
|
C
|
A:ASP342
|
4.9
|
28.1
|
1.0
|
N
|
A:ASP342
|
4.9
|
28.8
|
1.0
|
O
|
A:ALA340
|
5.0
|
29.6
|
1.0
|
|
Potassium binding site 2 out
of 6 in 1ynf
Go back to
Potassium Binding Sites List in 1ynf
Potassium binding site 2 out
of 6 in the Crystal Structure of N-Succinylarginine Dihydrolase, Astb, Bound to Substrate and Product, An Enzyme From the Arginine Catabolic Pathway of Escherichia Coli
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 N-Succinylarginine Dihydrolase, Astb, Bound to Substrate and Product, An Enzyme From the Arginine Catabolic Pathway of Escherichia Coli within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:K448
b:24.0
occ:1.00
|
O
|
B:ILE345
|
2.4
|
24.7
|
1.0
|
O
|
B:LEU339
|
2.7
|
26.1
|
1.0
|
OD1
|
B:ASN343
|
2.9
|
21.1
|
1.0
|
O
|
B:ALA341
|
3.0
|
27.9
|
1.0
|
O
|
B:HOH620
|
3.0
|
27.0
|
1.0
|
O
|
B:ASN343
|
3.0
|
25.7
|
1.0
|
O
|
B:LEU338
|
3.4
|
22.5
|
1.0
|
C
|
B:LEU339
|
3.4
|
25.6
|
1.0
|
C
|
B:ILE345
|
3.5
|
23.5
|
1.0
|
CG
|
B:ASN343
|
3.5
|
20.0
|
1.0
|
ND2
|
B:ASN343
|
3.8
|
14.5
|
1.0
|
C
|
B:ASN343
|
3.9
|
24.8
|
1.0
|
CA
|
B:LEU339
|
3.9
|
24.6
|
1.0
|
N
|
B:ASN343
|
4.0
|
27.2
|
1.0
|
N
|
B:ILE345
|
4.1
|
24.2
|
1.0
|
C
|
B:ALA341
|
4.1
|
29.0
|
1.0
|
CA
|
B:ILE345
|
4.2
|
22.4
|
1.0
|
N
|
B:ALA341
|
4.3
|
27.8
|
1.0
|
N
|
B:ALA340
|
4.3
|
25.1
|
1.0
|
C
|
B:LEU338
|
4.4
|
24.1
|
1.0
|
CA
|
B:ASN343
|
4.4
|
24.8
|
1.0
|
N
|
B:SER346
|
4.5
|
24.5
|
1.0
|
CB
|
B:ILE345
|
4.5
|
20.9
|
1.0
|
C
|
B:ALA340
|
4.5
|
27.7
|
1.0
|
CB
|
B:ASN343
|
4.5
|
22.9
|
1.0
|
C
|
B:PRO344
|
4.6
|
24.8
|
1.0
|
N
|
B:LEU339
|
4.6
|
23.1
|
1.0
|
O
|
B:HOH657
|
4.7
|
24.4
|
1.0
|
CA
|
B:SER346
|
4.7
|
24.8
|
1.0
|
CA
|
B:ALA340
|
4.7
|
26.3
|
1.0
|
CA
|
B:ALA341
|
4.8
|
28.9
|
1.0
|
N
|
B:PRO344
|
4.8
|
24.3
|
1.0
|
|
Potassium binding site 3 out
of 6 in 1ynf
Go back to
Potassium Binding Sites List in 1ynf
Potassium binding site 3 out
of 6 in the Crystal Structure of N-Succinylarginine Dihydrolase, Astb, Bound to Substrate and Product, An Enzyme From the Arginine Catabolic Pathway of Escherichia Coli
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 N-Succinylarginine Dihydrolase, Astb, Bound to Substrate and Product, An Enzyme From the Arginine Catabolic Pathway of Escherichia Coli within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:K448
b:31.3
occ:1.00
|
O
|
C:ALA341
|
2.6
|
33.9
|
1.0
|
O
|
C:ILE345
|
2.8
|
27.7
|
1.0
|
O
|
C:LEU339
|
2.9
|
32.2
|
1.0
|
OD1
|
C:ASN343
|
2.9
|
26.1
|
1.0
|
O
|
C:ASN343
|
3.0
|
26.0
|
1.0
|
O
|
C:LEU338
|
3.2
|
29.7
|
1.0
|
CG
|
C:ASN343
|
3.3
|
27.2
|
1.0
|
ND2
|
C:ASN343
|
3.5
|
24.0
|
1.0
|
C
|
C:LEU339
|
3.5
|
31.4
|
1.0
|
N
|
C:ASN343
|
3.7
|
29.6
|
1.0
|
C
|
C:ALA341
|
3.7
|
33.0
|
1.0
|
C
|
C:ASN343
|
3.7
|
27.9
|
1.0
|
C
|
C:ILE345
|
3.8
|
27.2
|
1.0
|
N
|
C:ALA341
|
4.1
|
31.3
|
1.0
|
CA
|
C:LEU339
|
4.1
|
30.4
|
1.0
|
CA
|
C:ASN343
|
4.1
|
27.9
|
1.0
|
N
|
C:ILE345
|
4.2
|
25.3
|
1.0
|
C
|
C:LEU338
|
4.3
|
29.9
|
1.0
|
CB
|
C:ASN343
|
4.3
|
26.6
|
1.0
|
O
|
C:HOH658
|
4.3
|
33.9
|
1.0
|
C
|
C:ALA340
|
4.3
|
31.1
|
1.0
|
N
|
C:ALA340
|
4.3
|
30.8
|
1.0
|
CA
|
C:ALA341
|
4.4
|
31.9
|
1.0
|
O
|
C:HOH626
|
4.4
|
51.0
|
1.0
|
CA
|
C:ILE345
|
4.4
|
25.7
|
1.0
|
CB
|
C:ILE345
|
4.6
|
26.5
|
1.0
|
CA
|
C:ALA340
|
4.6
|
30.4
|
1.0
|
N
|
C:ASP342
|
4.7
|
32.9
|
1.0
|
C
|
C:ASP342
|
4.7
|
31.5
|
1.0
|
N
|
C:LEU339
|
4.7
|
29.5
|
1.0
|
N
|
C:PRO344
|
4.8
|
26.9
|
1.0
|
C
|
C:PRO344
|
4.8
|
25.1
|
1.0
|
O
|
C:ALA340
|
4.8
|
31.8
|
1.0
|
CA
|
C:ASP342
|
4.8
|
33.2
|
1.0
|
N
|
C:SER346
|
4.9
|
27.9
|
1.0
|
|
Potassium binding site 4 out
of 6 in 1ynf
Go back to
Potassium Binding Sites List in 1ynf
Potassium binding site 4 out
of 6 in the Crystal Structure of N-Succinylarginine Dihydrolase, Astb, Bound to Substrate and Product, An Enzyme From the Arginine Catabolic Pathway of Escherichia Coli
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 N-Succinylarginine Dihydrolase, Astb, Bound to Substrate and Product, An Enzyme From the Arginine Catabolic Pathway of Escherichia Coli within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:K448
b:63.4
occ:1.00
|
O
|
D:ILE345
|
2.7
|
33.7
|
1.0
|
OD1
|
D:ASN343
|
2.7
|
37.5
|
1.0
|
O
|
D:ALA341
|
2.8
|
36.9
|
1.0
|
O
|
D:ASN343
|
2.8
|
31.9
|
1.0
|
O
|
D:LEU339
|
3.0
|
39.8
|
1.0
|
CG
|
D:ASN343
|
3.2
|
36.5
|
1.0
|
O
|
D:LEU338
|
3.3
|
34.8
|
1.0
|
ND2
|
D:ASN343
|
3.4
|
37.8
|
1.0
|
C
|
D:ASN343
|
3.6
|
33.4
|
1.0
|
C
|
D:ILE345
|
3.6
|
33.3
|
1.0
|
C
|
D:LEU339
|
3.7
|
38.1
|
1.0
|
N
|
D:ASN343
|
3.7
|
36.0
|
1.0
|
C
|
D:ALA341
|
3.9
|
35.7
|
1.0
|
N
|
D:ILE345
|
4.0
|
31.6
|
1.0
|
CA
|
D:ASN343
|
4.0
|
34.1
|
1.0
|
CA
|
D:LEU339
|
4.2
|
37.2
|
1.0
|
CB
|
D:ASN343
|
4.2
|
36.5
|
1.0
|
CA
|
D:ILE345
|
4.2
|
32.7
|
1.0
|
N
|
D:ALA341
|
4.3
|
37.1
|
1.0
|
C
|
D:LEU338
|
4.4
|
36.3
|
1.0
|
CB
|
D:ILE345
|
4.4
|
34.2
|
1.0
|
N
|
D:ALA340
|
4.5
|
38.5
|
1.0
|
C
|
D:PRO344
|
4.5
|
31.4
|
1.0
|
C
|
D:ALA340
|
4.6
|
37.4
|
1.0
|
N
|
D:PRO344
|
4.6
|
32.1
|
1.0
|
CA
|
D:ALA341
|
4.6
|
35.9
|
1.0
|
N
|
D:SER346
|
4.7
|
33.4
|
1.0
|
C
|
D:ASP342
|
4.7
|
36.5
|
1.0
|
N
|
D:LEU339
|
4.8
|
36.9
|
1.0
|
N
|
D:ASP342
|
4.8
|
36.9
|
1.0
|
CA
|
D:ALA340
|
4.9
|
37.9
|
1.0
|
CA
|
D:SER346
|
5.0
|
34.0
|
1.0
|
|
Potassium binding site 5 out
of 6 in 1ynf
Go back to
Potassium Binding Sites List in 1ynf
Potassium binding site 5 out
of 6 in the Crystal Structure of N-Succinylarginine Dihydrolase, Astb, Bound to Substrate and Product, An Enzyme From the Arginine Catabolic Pathway of Escherichia Coli
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 N-Succinylarginine Dihydrolase, Astb, Bound to Substrate and Product, An Enzyme From the Arginine Catabolic Pathway of Escherichia Coli within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:K448
b:27.8
occ:1.00
|
O
|
E:ALA341
|
2.7
|
35.2
|
1.0
|
O
|
E:ILE345
|
2.7
|
28.8
|
1.0
|
OD1
|
E:ASN343
|
2.8
|
27.4
|
1.0
|
O
|
E:LEU339
|
2.9
|
33.3
|
1.0
|
O
|
E:ASN343
|
3.0
|
27.1
|
1.0
|
O
|
E:LEU338
|
3.2
|
30.1
|
1.0
|
CG
|
E:ASN343
|
3.2
|
28.1
|
1.0
|
C
|
E:LEU339
|
3.5
|
31.9
|
1.0
|
ND2
|
E:ASN343
|
3.5
|
28.3
|
1.0
|
C
|
E:ASN343
|
3.7
|
28.7
|
1.0
|
N
|
E:ASN343
|
3.8
|
31.0
|
1.0
|
C
|
E:ILE345
|
3.8
|
27.5
|
1.0
|
C
|
E:ALA341
|
3.8
|
34.2
|
1.0
|
CA
|
E:LEU339
|
4.1
|
30.7
|
1.0
|
N
|
E:ALA341
|
4.1
|
33.4
|
1.0
|
CA
|
E:ASN343
|
4.1
|
29.2
|
1.0
|
N
|
E:ILE345
|
4.2
|
25.4
|
1.0
|
C
|
E:LEU338
|
4.2
|
30.3
|
1.0
|
CB
|
E:ASN343
|
4.3
|
28.3
|
1.0
|
O
|
E:HOH615
|
4.3
|
36.2
|
1.0
|
N
|
E:ALA340
|
4.3
|
31.8
|
1.0
|
CA
|
E:ILE345
|
4.4
|
26.7
|
1.0
|
C
|
E:ALA340
|
4.4
|
32.4
|
1.0
|
CA
|
E:ALA341
|
4.5
|
33.5
|
1.0
|
CB
|
E:ILE345
|
4.6
|
25.9
|
1.0
|
N
|
E:LEU339
|
4.6
|
29.5
|
1.0
|
CA
|
E:ALA340
|
4.7
|
31.0
|
1.0
|
C
|
E:PRO344
|
4.7
|
26.9
|
1.0
|
C
|
E:ASP342
|
4.7
|
33.0
|
1.0
|
N
|
E:PRO344
|
4.8
|
28.2
|
1.0
|
N
|
E:ASP342
|
4.8
|
34.3
|
1.0
|
N
|
E:SER346
|
4.8
|
28.0
|
1.0
|
O
|
E:ALA340
|
4.9
|
32.5
|
1.0
|
CA
|
E:ASP342
|
4.9
|
34.7
|
1.0
|
|
Potassium binding site 6 out
of 6 in 1ynf
Go back to
Potassium Binding Sites List in 1ynf
Potassium binding site 6 out
of 6 in the Crystal Structure of N-Succinylarginine Dihydrolase, Astb, Bound to Substrate and Product, An Enzyme From the Arginine Catabolic Pathway of Escherichia Coli
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 N-Succinylarginine Dihydrolase, Astb, Bound to Substrate and Product, An Enzyme From the Arginine Catabolic Pathway of Escherichia Coli within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:K448
b:51.5
occ:1.00
|
O
|
F:ILE345
|
2.7
|
34.0
|
1.0
|
O
|
F:ALA341
|
2.7
|
35.3
|
1.0
|
O
|
F:LEU339
|
2.8
|
38.0
|
1.0
|
OD1
|
F:ASN343
|
2.9
|
36.9
|
1.0
|
O
|
F:ASN343
|
3.0
|
32.9
|
1.0
|
O
|
F:LEU338
|
3.1
|
34.7
|
1.0
|
CG
|
F:ASN343
|
3.2
|
36.2
|
1.0
|
ND2
|
F:ASN343
|
3.3
|
36.3
|
1.0
|
C
|
F:LEU339
|
3.5
|
37.0
|
1.0
|
C
|
F:ILE345
|
3.7
|
33.2
|
1.0
|
C
|
F:ASN343
|
3.8
|
33.5
|
1.0
|
C
|
F:ALA341
|
3.8
|
35.7
|
1.0
|
N
|
F:ASN343
|
3.8
|
36.5
|
1.0
|
CA
|
F:LEU339
|
4.0
|
36.3
|
1.0
|
N
|
F:ALA341
|
4.1
|
36.0
|
1.0
|
N
|
F:ILE345
|
4.1
|
31.4
|
1.0
|
C
|
F:LEU338
|
4.1
|
35.6
|
1.0
|
CA
|
F:ASN343
|
4.2
|
34.8
|
1.0
|
CB
|
F:ASN343
|
4.3
|
36.9
|
1.0
|
CA
|
F:ILE345
|
4.3
|
32.4
|
1.0
|
N
|
F:ALA340
|
4.3
|
36.6
|
1.0
|
C
|
F:ALA340
|
4.4
|
36.4
|
1.0
|
CB
|
F:ILE345
|
4.5
|
33.2
|
1.0
|
CA
|
F:ALA341
|
4.5
|
35.0
|
1.0
|
N
|
F:LEU339
|
4.5
|
35.5
|
1.0
|
CA
|
F:ALA340
|
4.7
|
36.5
|
1.0
|
C
|
F:PRO344
|
4.7
|
32.0
|
1.0
|
N
|
F:SER346
|
4.8
|
33.8
|
1.0
|
N
|
F:PRO344
|
4.8
|
32.1
|
1.0
|
N
|
F:ASP342
|
4.8
|
36.7
|
1.0
|
C
|
F:ASP342
|
4.8
|
37.1
|
1.0
|
O
|
F:ALA340
|
5.0
|
36.2
|
1.0
|
|
Reference:
A.Tocilj,
J.D.Schrag,
Y.Li,
B.L.Schneider,
L.Reitzer,
A.Matte,
M.Cygler.
Crystal Structure of N-Succinylarginine Dihydrolase Astb, Bound to Substrate and Product, An Enzyme From the Arginine Catabolic Pathway of Escherichia Coli. J.Biol.Chem. V. 280 15800 2005.
ISSN: ISSN 0021-9258
PubMed: 15703173
DOI: 10.1074/JBC.M413833200
Page generated: Mon Aug 12 05:51:28 2024
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