Potassium in PDB 1guq: Structure of Nucleotidyltransferase Complexed with Udp-Glucose
Enzymatic activity of Structure of Nucleotidyltransferase Complexed with Udp-Glucose
All present enzymatic activity of Structure of Nucleotidyltransferase Complexed with Udp-Glucose:
2.7.7.10;
Protein crystallography data
The structure of Structure of Nucleotidyltransferase Complexed with Udp-Glucose, PDB code: 1guq
was solved by
J.B.Thoden,
I.Rayment,
H.Holden,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
30.00 /
1.80
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
68.400,
57.500,
188.900,
90.00,
100.13,
90.00
|
R / Rfree (%)
|
n/a /
n/a
|
Other elements in 1guq:
The structure of Structure of Nucleotidyltransferase Complexed with Udp-Glucose also contains other interesting chemical elements:
Potassium Binding Sites:
The binding sites of Potassium atom in the Structure of Nucleotidyltransferase Complexed with Udp-Glucose
(pdb code 1guq). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total 4 binding sites of Potassium where determined in the
Structure of Nucleotidyltransferase Complexed with Udp-Glucose, PDB code: 1guq:
Jump to Potassium binding site number:
1;
2;
3;
4;
Potassium binding site 1 out
of 4 in 1guq
Go back to
Potassium Binding Sites List in 1guq
Potassium binding site 1 out
of 4 in the Structure of Nucleotidyltransferase Complexed with Udp-Glucose
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 1 of Structure of Nucleotidyltransferase Complexed with Udp-Glucose within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K353
b:15.8
occ:1.00
|
O
|
A:GLY166
|
2.7
|
15.2
|
1.0
|
O
|
A:ASN153
|
2.7
|
12.7
|
1.0
|
O
|
A:HOH492
|
2.8
|
22.5
|
1.0
|
O
|
A:HOH503
|
2.8
|
17.9
|
1.0
|
O
|
A:HOH354
|
2.9
|
10.4
|
1.0
|
O
|
A:HOH394
|
2.9
|
15.2
|
1.0
|
O
|
A:HOH382
|
3.0
|
16.4
|
1.0
|
C
|
A:GLY166
|
3.7
|
16.8
|
1.0
|
O
|
A:HOH459
|
3.8
|
17.4
|
1.0
|
C
|
A:ASN153
|
3.8
|
10.9
|
1.0
|
N
|
A:GLY166
|
3.9
|
10.4
|
1.0
|
O
|
A:HIS164
|
4.1
|
21.2
|
1.0
|
O
|
A:HOH555
|
4.2
|
23.5
|
1.0
|
N
|
A:ASN153
|
4.3
|
17.9
|
1.0
|
CA
|
A:GLY166
|
4.3
|
10.7
|
1.0
|
CG
|
A:GLU152
|
4.4
|
11.2
|
1.0
|
CB
|
A:CYS160
|
4.4
|
16.7
|
1.0
|
O1A
|
A:UPG352
|
4.4
|
7.1
|
1.0
|
O
|
A:ASN162
|
4.5
|
20.2
|
1.0
|
CA
|
A:ASN153
|
4.6
|
9.3
|
1.0
|
O2A
|
A:UPG352
|
4.6
|
14.0
|
1.0
|
N
|
A:GLY167
|
4.7
|
14.0
|
1.0
|
OE2
|
A:GLU152
|
4.7
|
11.6
|
1.0
|
N
|
A:LYS154
|
4.7
|
13.3
|
1.0
|
CA
|
A:LYS154
|
4.7
|
11.3
|
1.0
|
C
|
A:PRO165
|
4.9
|
13.3
|
1.0
|
PA
|
A:UPG352
|
5.0
|
13.2
|
1.0
|
CB
|
A:ASN153
|
5.0
|
8.1
|
1.0
|
CA
|
A:GLY167
|
5.0
|
9.0
|
1.0
|
|
Potassium binding site 2 out
of 4 in 1guq
Go back to
Potassium Binding Sites List in 1guq
Potassium binding site 2 out
of 4 in the Structure of Nucleotidyltransferase Complexed with Udp-Glucose
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 2 of Structure of Nucleotidyltransferase Complexed with Udp-Glucose within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:K353
b:18.0
occ:1.00
|
O
|
B:ASN153
|
2.6
|
13.7
|
1.0
|
O
|
B:HOH372
|
2.7
|
19.5
|
1.0
|
O
|
B:GLY166
|
2.7
|
15.0
|
1.0
|
O
|
B:HOH360
|
2.9
|
17.8
|
1.0
|
O
|
B:HOH479
|
2.9
|
23.1
|
1.0
|
O
|
B:HOH427
|
3.0
|
22.2
|
1.0
|
O
|
B:HOH355
|
3.2
|
9.6
|
1.0
|
C
|
B:GLY166
|
3.7
|
25.9
|
1.0
|
C
|
B:ASN153
|
3.7
|
9.2
|
1.0
|
N
|
B:GLY166
|
3.9
|
14.0
|
1.0
|
O
|
B:HOH444
|
3.9
|
19.6
|
1.0
|
O
|
B:HIS164
|
4.1
|
17.8
|
1.0
|
O
|
B:HOH406
|
4.2
|
15.6
|
1.0
|
CB
|
B:CYS160
|
4.3
|
17.0
|
1.0
|
CA
|
B:GLY166
|
4.3
|
12.6
|
1.0
|
N
|
B:ASN153
|
4.4
|
13.5
|
1.0
|
CG
|
B:GLU152
|
4.4
|
17.5
|
1.0
|
O
|
B:ASN162
|
4.4
|
38.5
|
1.0
|
O1A
|
B:UPG352
|
4.5
|
13.0
|
1.0
|
CA
|
B:LYS154
|
4.6
|
10.1
|
1.0
|
CA
|
B:ASN153
|
4.6
|
11.8
|
1.0
|
N
|
B:LYS154
|
4.6
|
11.6
|
1.0
|
O2A
|
B:UPG352
|
4.6
|
23.9
|
1.0
|
N
|
B:GLY167
|
4.7
|
13.0
|
1.0
|
OE2
|
B:GLU152
|
4.9
|
16.8
|
1.0
|
CA
|
B:GLY167
|
4.9
|
18.2
|
1.0
|
CB
|
B:ASN153
|
5.0
|
18.1
|
1.0
|
C
|
B:PRO165
|
5.0
|
26.2
|
1.0
|
|
Potassium binding site 3 out
of 4 in 1guq
Go back to
Potassium Binding Sites List in 1guq
Potassium binding site 3 out
of 4 in the Structure of Nucleotidyltransferase Complexed with Udp-Glucose
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 3 of Structure of Nucleotidyltransferase Complexed with Udp-Glucose within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:K353
b:18.4
occ:1.00
|
O
|
C:ASN153
|
2.5
|
15.0
|
1.0
|
O
|
C:HOH925
|
2.6
|
19.4
|
1.0
|
O
|
C:GLY166
|
2.8
|
14.4
|
1.0
|
O
|
C:HOH877
|
2.9
|
16.0
|
1.0
|
O
|
C:HOH899
|
3.0
|
16.2
|
1.0
|
O
|
C:HOH957
|
3.1
|
20.2
|
1.0
|
O
|
C:HOH770
|
3.1
|
19.9
|
1.0
|
C
|
C:ASN153
|
3.7
|
18.3
|
1.0
|
O
|
C:HOH937
|
3.7
|
20.4
|
1.0
|
C
|
C:GLY166
|
3.8
|
22.6
|
1.0
|
N
|
C:GLY166
|
4.0
|
16.2
|
1.0
|
O
|
C:HIS164
|
4.2
|
17.0
|
1.0
|
N
|
C:ASN153
|
4.2
|
16.8
|
1.0
|
O
|
C:HOH793
|
4.2
|
25.7
|
1.0
|
CG
|
C:GLU152
|
4.4
|
11.9
|
1.0
|
O1A
|
C:UPG352
|
4.4
|
12.8
|
1.0
|
CA
|
C:GLY166
|
4.4
|
8.6
|
1.0
|
O
|
C:ASN162
|
4.5
|
20.9
|
1.0
|
CA
|
C:ASN153
|
4.5
|
17.0
|
1.0
|
CB
|
C:CYS160
|
4.5
|
14.2
|
1.0
|
N
|
C:LYS154
|
4.6
|
10.7
|
1.0
|
CA
|
C:LYS154
|
4.7
|
12.7
|
1.0
|
N
|
C:GLY167
|
4.7
|
12.3
|
1.0
|
O2A
|
C:UPG352
|
4.8
|
15.1
|
1.0
|
OE2
|
C:GLU152
|
4.9
|
13.4
|
1.0
|
CB
|
C:ASN153
|
4.9
|
5.6
|
1.0
|
CA
|
C:GLY167
|
5.0
|
10.7
|
1.0
|
|
Potassium binding site 4 out
of 4 in 1guq
Go back to
Potassium Binding Sites List in 1guq
Potassium binding site 4 out
of 4 in the Structure of Nucleotidyltransferase Complexed with Udp-Glucose
Mono view
Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 4 of Structure of Nucleotidyltransferase Complexed with Udp-Glucose within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:K353
b:20.6
occ:1.00
|
O
|
D:HOH955
|
2.7
|
19.9
|
1.0
|
O
|
D:ASN153
|
2.8
|
16.2
|
1.0
|
O
|
D:GLY166
|
2.8
|
13.6
|
1.0
|
O
|
D:HOH1050
|
2.9
|
29.1
|
1.0
|
O
|
D:HOH750
|
2.9
|
16.2
|
1.0
|
O
|
D:HOH743
|
3.0
|
15.4
|
1.0
|
O
|
D:HOH836
|
3.2
|
13.3
|
1.0
|
C
|
D:GLY166
|
3.8
|
37.6
|
1.0
|
O
|
D:HOH756
|
3.8
|
22.9
|
1.0
|
C
|
D:ASN153
|
3.8
|
19.4
|
1.0
|
N
|
D:GLY166
|
4.0
|
14.7
|
1.0
|
O
|
D:HIS164
|
4.2
|
24.3
|
1.0
|
O
|
D:HOH991
|
4.2
|
26.2
|
1.0
|
O1A
|
D:UPG352
|
4.3
|
24.7
|
1.0
|
N
|
D:ASN153
|
4.4
|
17.3
|
1.0
|
CA
|
D:GLY166
|
4.4
|
17.7
|
1.0
|
O
|
D:ASN162
|
4.6
|
23.9
|
1.0
|
CG
|
D:GLU152
|
4.6
|
11.5
|
1.0
|
CA
|
D:ASN153
|
4.7
|
20.9
|
1.0
|
N
|
D:LYS154
|
4.7
|
15.9
|
1.0
|
CA
|
D:LYS154
|
4.7
|
9.7
|
1.0
|
N
|
D:GLY167
|
4.7
|
19.2
|
1.0
|
CB
|
D:CYS160
|
4.7
|
20.8
|
1.0
|
O2A
|
D:UPG352
|
4.8
|
17.2
|
1.0
|
OE2
|
D:GLU152
|
4.8
|
15.0
|
1.0
|
C
|
D:PRO165
|
4.9
|
31.7
|
1.0
|
CB
|
D:ASN153
|
4.9
|
10.4
|
1.0
|
CA
|
D:GLY167
|
4.9
|
17.2
|
1.0
|
|
Reference:
J.B.Thoden,
F.J.Ruzicka,
P.A.Frey,
I.Rayment,
H.M.Holden.
Structural Analysis of the H166G Site-Directed Mutant of Galactose-1-Phosphate Uridylyltransferase Complexed with Either Udp-Glucose or Udp-Galactose: Detailed Description of the Nucleotide Sugar Binding Site. Biochemistry V. 36 1212 1997.
ISSN: ISSN 0006-2960
PubMed: 9063869
DOI: 10.1021/BI9626517
Page generated: Mon Aug 12 04:32:22 2024
|