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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:

Iron (Fe) 4 atoms
Zinc (Zn) 4 atoms

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: Sat Aug 9 01:56:25 2025

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