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Potassium in PDB 1gup: Structure of Nucleotidyltransferase Complexed with Udp- Galactose

Enzymatic activity of Structure of Nucleotidyltransferase Complexed with Udp- Galactose

All present enzymatic activity of Structure of Nucleotidyltransferase Complexed with Udp- Galactose:
2.7.7.10;

Protein crystallography data

The structure of Structure of Nucleotidyltransferase Complexed with Udp- Galactose, PDB code: 1gup 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 (°) 68.700, 57.700, 188.700, 90.00, 100.08, 90.00
R / Rfree (%) n/a / n/a

Other elements in 1gup:

The structure of Structure of Nucleotidyltransferase Complexed with Udp- Galactose 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- Galactose (pdb code 1gup). 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- Galactose, PDB code: 1gup:
Jump to Potassium binding site number: 1; 2; 3; 4;

Potassium binding site 1 out of 4 in 1gup

Go back to Potassium Binding Sites List in 1gup
Potassium binding site 1 out of 4 in the Structure of Nucleotidyltransferase Complexed with Udp- Galactose


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- Galactose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K353

b:21.8
occ:1.00
O B:ASN153 2.5 10.8 1.0
O B:GLY166 2.7 13.0 1.0
O B:HOH458 2.8 21.6 1.0
O B:HOH376 3.0 19.3 1.0
O B:HOH430 3.0 33.0 1.0
O B:HOH354 3.2 8.7 1.0
O B:HOH422 3.3 22.7 1.0
C B:GLY166 3.7 17.7 1.0
C B:ASN153 3.7 14.5 1.0
O B:HOH457 3.9 23.6 1.0
N B:GLY166 4.1 14.6 1.0
N B:ASN153 4.2 11.2 1.0
O B:HIS164 4.2 21.7 1.0
O2A B:GDU352 4.3 43.7 1.0
CB B:CYS160 4.3 14.9 1.0
O B:HOH391 4.4 21.5 1.0
CG B:GLU152 4.4 7.6 1.0
CA B:GLY166 4.4 13.8 1.0
CA B:ASN153 4.5 9.3 1.0
N B:LYS154 4.6 23.2 1.0
N B:GLY167 4.6 14.1 1.0
O1A B:GDU352 4.6 27.6 1.0
CA B:LYS154 4.6 12.3 1.0
O B:ASN162 4.7 61.1 1.0
CA B:GLY167 4.8 15.2 1.0
OE2 B:GLU152 4.9 17.9 1.0
CB B:ASN153 5.0 22.2 1.0
PA B:GDU352 5.0 40.2 1.0

Potassium binding site 2 out of 4 in 1gup

Go back to Potassium Binding Sites List in 1gup
Potassium binding site 2 out of 4 in the Structure of Nucleotidyltransferase Complexed with Udp- Galactose


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- Galactose within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K353

b:17.5
occ:1.00
O A:GLY166 2.6 19.5 1.0
O A:ASN153 2.6 16.5 1.0
O A:HOH408 2.8 12.9 1.0
O A:HOH433 2.9 22.7 1.0
O A:HOH459 3.0 21.6 1.0
O A:HOH675 3.0 31.9 1.0
O A:HOH356 3.0 12.9 1.0
C A:GLY166 3.6 12.1 1.0
C A:ASN153 3.7 13.8 1.0
O A:HOH418 3.8 18.5 1.0
N A:GLY166 3.9 16.0 1.0
O A:HIS164 4.0 13.0 1.0
O A:HOH368 4.2 21.5 1.0
CA A:GLY166 4.3 12.3 1.0
N A:ASN153 4.3 19.7 1.0
CB A:CYS160 4.4 16.3 1.0
CG A:GLU152 4.5 14.6 1.0
O2A A:GDU352 4.5 32.4 1.0
O A:ASN162 4.6 27.6 1.0
CA A:ASN153 4.6 9.6 1.0
O1A A:GDU352 4.6 14.2 1.0
N A:LYS154 4.6 24.8 1.0
N A:GLY167 4.7 11.4 1.0
CA A:LYS154 4.7 10.8 1.0
OE2 A:GLU152 4.8 14.0 1.0
CB A:ASN153 4.9 28.1 1.0
C A:PRO165 5.0 13.3 1.0

Potassium binding site 3 out of 4 in 1gup

Go back to Potassium Binding Sites List in 1gup
Potassium binding site 3 out of 4 in the Structure of Nucleotidyltransferase Complexed with Udp- Galactose


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- Galactose within 5.0Å range:
probe atom residue distance (Å) B Occ
C:K353

b:21.8
occ:1.00
O C:HOH746 2.4 25.8 1.0
O C:ASN153 2.5 21.5 1.0
O C:GLY166 2.8 18.0 1.0
O C:HOH729 2.9 17.1 1.0
O C:HOH863 2.9 29.5 1.0
O C:HOH777 3.0 26.5 1.0
O C:HOH713 3.1 14.5 1.0
O C:HOH862 3.6 29.0 1.0
C C:ASN153 3.7 24.4 1.0
C C:GLY166 3.9 22.4 1.0
O C:HIS164 3.9 22.2 1.0
N C:GLY166 4.1 24.5 1.0
N C:ASN153 4.3 26.1 1.0
O1A C:GDU352 4.3 22.1 1.0
O C:ASN162 4.4 70.2 1.0
CG C:GLU152 4.4 14.4 1.0
O C:HOH759 4.4 18.1 1.0
CB C:CYS160 4.4 24.8 1.0
CA C:ASN153 4.5 22.2 1.0
CA C:GLY166 4.6 22.4 1.0
O2A C:GDU352 4.7 62.7 1.0
N C:LYS154 4.7 23.4 1.0
N C:GLY167 4.8 15.4 1.0
CA C:LYS154 4.8 23.1 1.0
CA C:GLY167 4.9 12.2 1.0
OE2 C:GLU152 4.9 20.2 1.0
CB C:ASN153 4.9 13.4 1.0

Potassium binding site 4 out of 4 in 1gup

Go back to Potassium Binding Sites List in 1gup
Potassium binding site 4 out of 4 in the Structure of Nucleotidyltransferase Complexed with Udp- Galactose


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- Galactose within 5.0Å range:
probe atom residue distance (Å) B Occ
D:K353

b:25.7
occ:1.00
O D:ASN153 2.5 20.6 1.0
O D:HOH741 2.6 25.6 1.0
O D:GLY166 2.8 19.3 1.0
O D:HOH719 3.0 22.0 1.0
O D:HOH783 3.1 25.5 1.0
O D:HOH701 3.2 15.0 1.0
C D:ASN153 3.6 53.3 1.0
C D:GLY166 3.8 39.0 1.0
O D:HOH984 4.0 30.4 1.0
N D:GLY166 4.0 22.0 1.0
O D:HIS164 4.1 30.1 1.0
O D:HOH765 4.2 39.0 1.0
N D:ASN153 4.2 14.1 1.0
CB D:CYS160 4.3 35.1 1.0
O1A D:GDU352 4.4 70.8 1.0
CA D:ASN153 4.4 25.6 1.0
O D:ASN162 4.4 85.5 1.0
CA D:GLY166 4.5 24.6 1.0
CG D:GLU152 4.5 18.1 1.0
N D:LYS154 4.5 19.6 1.0
CA D:LYS154 4.5 21.7 1.0
OE2 D:GLU152 4.6 21.8 1.0
CB D:ASN153 4.7 42.8 1.0
N D:GLY167 4.8 33.2 1.0
O2A D:GDU352 4.8 54.6 1.0
CA D:GLY167 5.0 31.6 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: Sun Dec 13 22:43:45 2020

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