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Magnesium in PDB 3c4v: Structure of the Retaining Glycosyltransferase Msha:the First Step in Mycothiol Biosynthesis. Organism: Corynebacterium Glutamicum : Complex with Udp and 1L-Ins-1- P.

Protein crystallography data

The structure of Structure of the Retaining Glycosyltransferase Msha:the First Step in Mycothiol Biosynthesis. Organism: Corynebacterium Glutamicum : Complex with Udp and 1L-Ins-1- P., PDB code: 3c4v was solved by M.W.Vetting, P.A.Frantom, J.S.Blanchard, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 79.18 / 2.60
Space group I 4 2 2
Cell size a, b, c (Å), α, β, γ (°) 223.940, 223.940, 125.005, 90.00, 90.00, 90.00
R / Rfree (%) 19 / 21.3

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of the Retaining Glycosyltransferase Msha:the First Step in Mycothiol Biosynthesis. Organism: Corynebacterium Glutamicum : Complex with Udp and 1L-Ins-1- P. (pdb code 3c4v). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structure of the Retaining Glycosyltransferase Msha:the First Step in Mycothiol Biosynthesis. Organism: Corynebacterium Glutamicum : Complex with Udp and 1L-Ins-1- P., PDB code: 3c4v:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 3c4v

Go back to Magnesium Binding Sites List in 3c4v
Magnesium binding site 1 out of 2 in the Structure of the Retaining Glycosyltransferase Msha:the First Step in Mycothiol Biosynthesis. Organism: Corynebacterium Glutamicum : Complex with Udp and 1L-Ins-1- P.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of the Retaining Glycosyltransferase Msha:the First Step in Mycothiol Biosynthesis. Organism: Corynebacterium Glutamicum : Complex with Udp and 1L-Ins-1- P. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg602

b:41.9
occ:1.00
O A:ALA306 2.3 41.8 1.0
O A:HOH608 2.3 29.3 1.0
OG1 A:THR330 2.4 42.2 1.0
O A:TYR303 2.9 40.8 1.0
O A:ARG304 3.0 41.8 1.0
O A:HOH634 3.0 42.8 1.0
CB A:THR330 3.5 43.1 1.0
C A:ALA306 3.5 42.2 1.0
C A:ARG304 3.5 41.2 1.0
CG2 A:THR330 3.6 41.6 1.0
CA A:ARG304 3.7 40.4 1.0
C A:TYR303 4.0 40.6 1.0
N A:ALA306 4.1 41.1 1.0
CA A:THR330 4.1 43.0 1.0
O A:GLY329 4.2 43.3 1.0
CA A:ALA306 4.2 41.6 1.0
N A:ARG304 4.3 40.7 1.0
OG1 A:THR210 4.3 51.2 1.0
O A:SER328 4.5 44.9 1.0
C A:GLY329 4.5 43.1 1.0
N A:ASP307 4.5 42.6 1.0
N A:THR330 4.5 42.7 1.0
N A:ALA305 4.6 41.2 1.0
C A:ALA305 4.6 41.2 1.0
CA A:ASP307 4.7 43.8 1.0
CB A:ALA306 4.7 40.9 1.0
OG A:SER328 4.9 48.7 1.0
CB A:ARG304 5.0 40.0 1.0

Magnesium binding site 2 out of 2 in 3c4v

Go back to Magnesium Binding Sites List in 3c4v
Magnesium binding site 2 out of 2 in the Structure of the Retaining Glycosyltransferase Msha:the First Step in Mycothiol Biosynthesis. Organism: Corynebacterium Glutamicum : Complex with Udp and 1L-Ins-1- P.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of the Retaining Glycosyltransferase Msha:the First Step in Mycothiol Biosynthesis. Organism: Corynebacterium Glutamicum : Complex with Udp and 1L-Ins-1- P. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg602

b:46.9
occ:1.00
O B:HOH607 2.4 39.7 1.0
O B:ALA306 2.4 41.8 1.0
OG1 B:THR330 2.5 42.6 1.0
O B:HOH629 2.8 35.2 1.0
O B:ARG304 2.9 42.5 1.0
O B:TYR303 3.0 41.2 1.0
C B:ARG304 3.4 41.2 1.0
CB B:THR330 3.6 42.3 1.0
C B:ALA306 3.6 41.9 1.0
CA B:ARG304 3.7 40.3 1.0
CG2 B:THR330 3.8 41.1 1.0
C B:TYR303 4.0 41.4 1.0
N B:ALA306 4.1 40.7 1.0
O B:GLY329 4.1 44.3 1.0
O B:HOH632 4.1 38.1 1.0
CA B:THR330 4.2 42.3 1.0
N B:ARG304 4.3 40.9 1.0
CA B:ALA306 4.4 41.4 1.0
OG1 B:THR210 4.4 47.8 1.0
N B:ALA305 4.5 41.1 1.0
C B:ALA305 4.5 40.8 1.0
C B:GLY329 4.6 43.5 1.0
N B:THR330 4.6 42.6 1.0
N B:ASP307 4.6 42.1 1.0
O B:HOH630 4.7 44.5 1.0
O B:SER328 4.7 45.4 1.0
CA B:ASP307 4.8 43.2 1.0
CB B:ALA306 4.9 41.5 1.0
CB B:ARG304 4.9 39.5 1.0

Reference:

M.W.Vetting, P.A.Frantom, J.S.Blanchard. Structural and Enzymatic Analysis of Msha From Corynebacterium Glutamicum: Substrate-Assisted Catalysis J.Biol.Chem. V. 283 15834 2008.
ISSN: ISSN 0021-9258
PubMed: 18390549
DOI: 10.1074/JBC.M801017200
Page generated: Wed Aug 14 09:26:12 2024

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