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Magnesium in PDB 3dk5: Crystal Structure of Apo-Glmu From Mycobacterium Tuberculosis

Enzymatic activity of Crystal Structure of Apo-Glmu From Mycobacterium Tuberculosis

All present enzymatic activity of Crystal Structure of Apo-Glmu From Mycobacterium Tuberculosis:
2.3.1.157; 2.7.7.23;

Protein crystallography data

The structure of Crystal Structure of Apo-Glmu From Mycobacterium Tuberculosis, PDB code: 3dk5 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) 29.30 / 2.23
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 79.600, 79.600, 278.000, 90.00, 90.00, 120.00
R / Rfree (%) 22.5 / 27.1

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Apo-Glmu From Mycobacterium Tuberculosis (pdb code 3dk5). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of Apo-Glmu From Mycobacterium Tuberculosis, PDB code: 3dk5:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 3dk5

Go back to Magnesium Binding Sites List in 3dk5
Magnesium binding site 1 out of 2 in the Crystal Structure of Apo-Glmu From Mycobacterium Tuberculosis


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 Apo-Glmu From Mycobacterium Tuberculosis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg496

b:18.0
occ:0.33
OD2 A:ASP417 2.6 27.5 1.0
O A:HOH530 3.6 26.5 1.0
CG A:ASP417 3.7 32.6 1.0
OD1 A:ASP417 4.0 36.5 1.0

Magnesium binding site 2 out of 2 in 3dk5

Go back to Magnesium Binding Sites List in 3dk5
Magnesium binding site 2 out of 2 in the Crystal Structure of Apo-Glmu From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Apo-Glmu From Mycobacterium Tuberculosis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg497

b:26.3
occ:0.33
OD1 A:ASP417 3.1 36.5 1.0
OG A:SER392 3.8 37.2 1.0
CG A:ASP417 4.2 32.6 1.0
OD2 A:ASP417 4.7 27.5 1.0
O A:SER392 4.9 25.9 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: Mon Dec 14 08:04:18 2020

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