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Magnesium in PDB 1tw1: Beta-1,4-Galactosyltransferase Mutant MET344HIS (M344H-Gal- T1) Complex with Udp-Galactose and Magnesium

Enzymatic activity of Beta-1,4-Galactosyltransferase Mutant MET344HIS (M344H-Gal- T1) Complex with Udp-Galactose and Magnesium

All present enzymatic activity of Beta-1,4-Galactosyltransferase Mutant MET344HIS (M344H-Gal- T1) Complex with Udp-Galactose and Magnesium:
2.4.1.22; 2.4.1.38; 2.4.1.90;

Protein crystallography data

The structure of Beta-1,4-Galactosyltransferase Mutant MET344HIS (M344H-Gal- T1) Complex with Udp-Galactose and Magnesium, PDB code: 1tw1 was solved by B.Ramakrishnan, E.Boeggeman, P.K.Qasba, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 37.38 / 2.30
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 50.006, 91.517, 142.751, 90.00, 90.00, 90.00
R / Rfree (%) 19.6 / 26.1

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Beta-1,4-Galactosyltransferase Mutant MET344HIS (M344H-Gal- T1) Complex with Udp-Galactose and Magnesium (pdb code 1tw1). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Beta-1,4-Galactosyltransferase Mutant MET344HIS (M344H-Gal- T1) Complex with Udp-Galactose and Magnesium, PDB code: 1tw1:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 1tw1

Go back to Magnesium Binding Sites List in 1tw1
Magnesium binding site 1 out of 2 in the Beta-1,4-Galactosyltransferase Mutant MET344HIS (M344H-Gal- T1) Complex with Udp-Galactose and Magnesium


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Beta-1,4-Galactosyltransferase Mutant MET344HIS (M344H-Gal- T1) Complex with Udp-Galactose and Magnesium within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1

b:22.6
occ:1.00
O A:HOH1420 2.0 18.3 1.0
O1A A:GDU2 2.0 30.9 1.0
OD1 A:ASP254 2.1 27.6 1.0
NE2 A:HIS344 2.1 38.5 1.0
O1B A:GDU2 2.2 25.7 1.0
NE2 A:HIS347 2.4 34.7 1.0
CG A:ASP254 3.0 28.6 1.0
CE1 A:HIS344 3.0 38.7 1.0
CD2 A:HIS344 3.2 37.2 1.0
CD2 A:HIS347 3.3 35.2 1.0
OD2 A:ASP254 3.3 29.0 1.0
CE1 A:HIS347 3.4 36.9 1.0
PB A:GDU2 3.4 27.5 1.0
PA A:GDU2 3.4 32.4 1.0
O3A A:GDU2 3.7 29.1 1.0
O3B A:GDU2 4.0 29.3 1.0
O A:HOH982 4.0 28.9 1.0
O2A A:GDU2 4.1 34.1 1.0
O3D A:GDU2 4.2 28.8 1.0
ND1 A:HIS344 4.2 38.5 1.0
CB A:ASP254 4.3 28.8 1.0
CG A:HIS344 4.3 37.0 1.0
CG A:HIS347 4.4 35.0 1.0
ND1 A:HIS347 4.5 36.2 1.0
NZ A:LYS279 4.5 27.2 1.0
NH2 A:ARG191 4.6 29.9 1.0
O2B A:GDU2 4.7 30.5 1.0
NH1 A:ARG191 4.7 33.0 1.0
OD2 A:ASP252 4.7 27.0 1.0
C3D A:GDU2 4.7 26.6 1.0
O5D A:GDU2 4.7 32.4 1.0
C5D A:GDU2 4.8 29.5 1.0
O A:ILE345 5.0 36.6 1.0

Magnesium binding site 2 out of 2 in 1tw1

Go back to Magnesium Binding Sites List in 1tw1
Magnesium binding site 2 out of 2 in the Beta-1,4-Galactosyltransferase Mutant MET344HIS (M344H-Gal- T1) Complex with Udp-Galactose and Magnesium


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Beta-1,4-Galactosyltransferase Mutant MET344HIS (M344H-Gal- T1) Complex with Udp-Galactose and Magnesium within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg403

b:24.4
occ:1.00
O1A B:GDU404 1.8 23.9 1.0
NE2 B:HIS347 2.0 34.3 1.0
O1B B:GDU404 2.1 24.7 1.0
OD1 B:ASP254 2.1 28.3 1.0
NE2 B:HIS344 2.1 31.2 1.0
O B:HOH905 2.2 20.7 1.0
CE1 B:HIS347 3.0 35.5 1.0
CE1 B:HIS344 3.0 31.0 1.0
CD2 B:HIS347 3.1 33.3 1.0
CG B:ASP254 3.1 27.0 1.0
CD2 B:HIS344 3.2 31.3 1.0
PA B:GDU404 3.3 24.6 1.0
PB B:GDU404 3.3 25.0 1.0
OD2 B:ASP254 3.5 26.0 1.0
O3A B:GDU404 3.5 24.4 1.0
O3B B:GDU404 3.9 25.1 1.0
O2A B:GDU404 3.9 27.4 1.0
O3D B:GDU404 4.0 27.1 1.0
ND1 B:HIS347 4.1 35.1 1.0
ND1 B:HIS344 4.2 30.2 1.0
O B:HOH952 4.2 28.1 1.0
CG B:HIS347 4.2 35.7 1.0
CG B:HIS344 4.3 31.5 1.0
NH2 B:ARG191 4.3 29.3 1.0
CB B:ASP254 4.4 24.6 1.0
NZ B:LYS279 4.5 35.0 1.0
O2B B:GDU404 4.5 25.4 1.0
O5D B:GDU404 4.5 26.1 1.0
NH1 B:ARG191 4.6 28.2 1.0
C3D B:GDU404 4.6 25.6 1.0
OD2 B:ASP252 4.7 24.8 1.0
C5D B:GDU404 4.7 24.8 1.0
CZ B:ARG191 5.0 30.0 1.0

Reference:

B.Ramakrishnan, E.Boeggeman, P.K.Qasba. Effect of the MET344HIS Mutation on the Conformational Dynamics of Bovine Beta-1,4-Galactosyltransferase: Crystal Structure of the MET344HIS Mutant in Complex with Chitobiose Biochemistry V. 43 12513 2004.
ISSN: ISSN 0006-2960
PubMed: 15449940
DOI: 10.1021/BI049007+
Page generated: Tue Aug 13 14:39:53 2024

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