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Magnesium in PDB 5cak: Crystal Structure of Mycobacterium Tuberculosis Malate Synthase in Complex with 2-Hydroxy-3-(1H-Indol-3-Yl)Propanoic Acid

Enzymatic activity of Crystal Structure of Mycobacterium Tuberculosis Malate Synthase in Complex with 2-Hydroxy-3-(1H-Indol-3-Yl)Propanoic Acid

All present enzymatic activity of Crystal Structure of Mycobacterium Tuberculosis Malate Synthase in Complex with 2-Hydroxy-3-(1H-Indol-3-Yl)Propanoic Acid:
2.3.3.9;

Protein crystallography data

The structure of Crystal Structure of Mycobacterium Tuberculosis Malate Synthase in Complex with 2-Hydroxy-3-(1H-Indol-3-Yl)Propanoic Acid, PDB code: 5cak was solved by H.-L.Huang, J.C.Sacchettini, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.58 / 1.99
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 78.238, 78.238, 223.566, 90.00, 90.00, 90.00
R / Rfree (%) 16.4 / 22.1

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Mycobacterium Tuberculosis Malate Synthase in Complex with 2-Hydroxy-3-(1H-Indol-3-Yl)Propanoic Acid (pdb code 5cak). 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 Mycobacterium Tuberculosis Malate Synthase in Complex with 2-Hydroxy-3-(1H-Indol-3-Yl)Propanoic Acid, PDB code: 5cak:

Magnesium binding site 1 out of 1 in 5cak

Go back to Magnesium Binding Sites List in 5cak
Magnesium binding site 1 out of 1 in the Crystal Structure of Mycobacterium Tuberculosis Malate Synthase in Complex with 2-Hydroxy-3-(1H-Indol-3-Yl)Propanoic Acid


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 Mycobacterium Tuberculosis Malate Synthase in Complex with 2-Hydroxy-3-(1H-Indol-3-Yl)Propanoic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg801

b:11.9
occ:1.00
 OD2 A:ASP462 2.0 13.3 1.0
O A:HOH1089 2.0 10.3 1.0
OE2 A:GLU434 2.1 11.7 1.0
O A:HOH902 2.1 20.2 1.0
O A:HOH1013 2.1 10.9 1.0
O A:HOH1324 2.1 22.0 1.0
CG A:ASP462 3.0 12.9 1.0
CD A:GLU434 3.1 11.2 1.0
CB A:ASP462 3.4 14.0 1.0
OE1 A:GLU434 3.4 10.2 1.0
O14 A:4Z9802 3.9 26.0 1.0
NZ A:LYS399 3.9 11.1 1.0
O A:HOH903 4.0 30.0 1.0
NH1 A:ARG339 4.0 12.3 1.0
OD1 A:ASP462 4.0 8.3 1.0
OD2 A:ASP274 4.1 11.9 1.0
O A:HOH1362 4.1 26.8 1.0
O12 A:4Z9802 4.3 28.4 1.0
CG A:GLU434 4.4 9.2 1.0
CB A:ALA635 4.4 11.5 1.0
OE1 A:GLU273 4.5 11.1 1.0
OD2 A:ASP633 4.6 18.5 1.0
CE A:MET432 4.6 28.9 1.0
CA A:ASP462 4.7 14.2 1.0
CB A:GLU434 4.7 10.9 1.0
N A:ASP462 4.8 16.7 1.0
CG A:ASP274 4.9 11.8 1.0
O A:HOH1337 5.0 15.7 1.0

Reference:

H.L.Huang, I.V.Krieger, M.K.Parai, V.B.Gawandi, J.C.Sacchettini. Mycobacterium Tuberculosis Malate Synthase Structures with Fragments Reveal A Portal For Substrate/Product Exchange. J. Biol. Chem. V. 291 27421 2016.
ISSN: ESSN 1083-351X
PubMed: 27738104
DOI: 10.1074/JBC.M116.750877
Page generated: Sun Sep 29 02:02:14 2024

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