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Sodium in PDB 1kvs: Udp-Galactose 4-Epimerase Complexed with Udp-Phenol

Enzymatic activity of Udp-Galactose 4-Epimerase Complexed with Udp-Phenol

All present enzymatic activity of Udp-Galactose 4-Epimerase Complexed with Udp-Phenol:
5.1.3.2;

Protein crystallography data

The structure of Udp-Galactose 4-Epimerase Complexed with Udp-Phenol, PDB code: 1kvs was solved by J.B.Thoden, A.M.Gulick, H.M.Holden, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.15
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 83.500, 83.500, 108.400, 90.00, 90.00, 120.00
R / Rfree (%) n/a / n/a

Sodium Binding Sites:

The binding sites of Sodium atom in the Udp-Galactose 4-Epimerase Complexed with Udp-Phenol (pdb code 1kvs). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Udp-Galactose 4-Epimerase Complexed with Udp-Phenol, PDB code: 1kvs:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in 1kvs

Go back to Sodium Binding Sites List in 1kvs
Sodium binding site 1 out of 2 in the Udp-Galactose 4-Epimerase Complexed with Udp-Phenol


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Udp-Galactose 4-Epimerase Complexed with Udp-Phenol within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na412

b:33.5
occ:1.00
OE1 A:GLN91 2.4 14.8 1.0
O A:HOH489 2.6 33.3 1.0
CD A:GLN91 3.4 49.7 1.0
NE2 A:GLN91 3.9 20.2 1.0
O A:HOH490 3.9 29.0 1.0
CA A:GLN91 4.6 41.9 1.0
CG A:GLN91 4.7 16.8 1.0
O A:VAL90 4.7 24.2 1.0
CB A:GLN91 4.7 31.5 1.0

Sodium binding site 2 out of 2 in 1kvs

Go back to Sodium Binding Sites List in 1kvs
Sodium binding site 2 out of 2 in the Udp-Galactose 4-Epimerase Complexed with Udp-Phenol


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of Udp-Galactose 4-Epimerase Complexed with Udp-Phenol within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na413

b:17.8
occ:1.00
O A:HOH580 2.4 38.1 1.0
O A:HOH579 2.4 29.5 1.0
O A:ILE196 2.9 29.2 1.0
O A:GLN194 3.2 30.2 1.0
O A:HOH479 3.2 41.7 1.0
O A:HOH442 3.6 20.4 1.0
C A:ILE196 3.7 42.3 1.0
O A:HOH443 3.9 45.7 1.0
O A:HOH486 4.0 30.9 1.0
OD1 A:ASN198 4.1 35.0 1.0
CB A:PRO193 4.1 13.2 1.0
CA A:PRO197 4.1 21.4 1.0
C A:GLN194 4.2 59.2 1.0
N A:PRO197 4.3 33.5 1.0
N A:ASN198 4.4 47.3 1.0
N A:GLN194 4.4 22.7 1.0
N A:ILE196 4.5 13.8 1.0
CG A:ASN198 4.5 79.8 1.0
C A:GLY195 4.6 21.7 1.0
C A:PRO197 4.6 44.9 1.0
O A:HOH723 4.7 49.0 1.0
C A:PRO193 4.8 53.7 1.0
O A:HOH477 4.8 23.7 1.0
CA A:PRO193 4.8 27.4 1.0
CA A:ILE196 4.8 25.8 1.0
O A:GLY195 4.9 15.6 1.0
ND2 A:ASN198 4.9 14.8 1.0
O A:HOH573 4.9 30.4 1.0
CA A:GLN194 5.0 24.2 1.0
CA A:GLY195 5.0 13.9 1.0

Reference:

J.B.Thoden, A.M.Gulick, H.M.Holden. Molecular Structures of the S124A, S124T, and S124V Site-Directed Mutants of Udp-Galactose 4-Epimerase From Escherichia Coli. Biochemistry V. 36 10685 1997.
ISSN: ISSN 0006-2960
PubMed: 9271499
DOI: 10.1021/BI9704313
Page generated: Sun Aug 17 06:09:09 2025

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