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Magnesium in PDB 3dj4: Crystal Structure of Glmu From Mycobacterium Tuberculosis in Complex with Uridine-Diphosphate-N-Acetylglucosamine.

Enzymatic activity of Crystal Structure of Glmu From Mycobacterium Tuberculosis in Complex with Uridine-Diphosphate-N-Acetylglucosamine.

All present enzymatic activity of Crystal Structure of Glmu From Mycobacterium Tuberculosis in Complex with Uridine-Diphosphate-N-Acetylglucosamine.:
2.3.1.157; 2.7.7.23;

Protein crystallography data

The structure of Crystal Structure of Glmu From Mycobacterium Tuberculosis in Complex with Uridine-Diphosphate-N-Acetylglucosamine., PDB code: 3dj4 was solved by S.K.Verma, B.Prakash, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.03 / 2.38
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 78.600, 78.600, 278.000, 90.00, 90.00, 120.00
R / Rfree (%) 19.4 / 25.7

Other elements in 3dj4:

The structure of Crystal Structure of Glmu From Mycobacterium Tuberculosis in Complex with Uridine-Diphosphate-N-Acetylglucosamine. also contains other interesting chemical elements:

Cobalt (Co) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Glmu From Mycobacterium Tuberculosis in Complex with Uridine-Diphosphate-N-Acetylglucosamine. (pdb code 3dj4). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of Glmu From Mycobacterium Tuberculosis in Complex with Uridine-Diphosphate-N-Acetylglucosamine., PDB code: 3dj4:

Magnesium binding site 1 out of 1 in 3dj4

Go back to Magnesium Binding Sites List in 3dj4
Magnesium binding site 1 out of 1 in the Crystal Structure of Glmu From Mycobacterium Tuberculosis in Complex with Uridine-Diphosphate-N-Acetylglucosamine.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Glmu From Mycobacterium Tuberculosis in Complex with Uridine-Diphosphate-N-Acetylglucosamine. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg496

b:5.6
occ:1.00
 O1B A:UD14000 2.0 17.1 1.0
OD1 A:ASN239 2.0 18.4 1.0
OD2 A:ASP114 2.0 14.3 1.0
O A:HOH4133 2.1 13.3 1.0
O2A A:UD14000 2.1 19.1 1.0
O A:HOH4120 2.3 15.6 1.0
CG A:ASN239 2.9 14.9 1.0
CG A:ASP114 3.1 17.7 1.0
PA A:UD14000 3.2 13.3 1.0
ND2 A:ASN239 3.2 8.2 1.0
PB A:UD14000 3.5 12.8 1.0
OD1 A:ASP114 3.5 11.4 1.0
NZ A:LYS26 3.8 9.2 1.0
O3A A:UD14000 3.9 17.9 1.0
O6' A:UD14000 4.1 14.6 1.0
O5B A:UD14000 4.3 15.8 1.0
C5B A:UD14000 4.3 21.0 1.0
O5' A:UD14000 4.3 17.6 1.0
CB A:ASN239 4.4 14.3 1.0
O1A A:UD14000 4.4 20.3 1.0
O1' A:UD14000 4.4 19.5 1.0
CB A:ASP114 4.4 17.4 1.0
O2B A:UD14000 4.5 19.2 1.0
O A:VAL238 4.5 15.4 1.0
O A:HOH4110 4.5 16.2 1.0
C1' A:UD14000 4.7 18.8 1.0
C A:VAL238 4.7 16.5 1.0
CA A:ASN239 4.7 14.7 1.0
CE A:LYS26 4.8 14.9 1.0
C3B A:UD14000 4.8 20.0 1.0
N A:ASN239 4.8 15.0 1.0
N A:VAL238 5.0 17.8 1.0
C5' A:UD14000 5.0 20.9 1.0
C4B A:UD14000 5.0 18.4 1.0

Reference:

A.Parikh, S.K.Verma, S.Khan, B.Prakash, V.K.Nandicoori. Pknb-Mediated Phosphorylation of A Novel Substrate, N-Acetylglucosamine-1-Phosphate Uridyltransferase, Modulates Its Acetyltransferase Activity. J.Mol.Biol. V. 386 451 2009.
ISSN: ISSN 0022-2836
PubMed: 19121323
DOI: 10.1016/J.JMB.2008.12.031
Page generated: Wed Aug 14 12:32:07 2024

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