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Magnesium in PDB 1n8i: Biochemical and Structural Studies of Malate Synthase From Mycobacterium Tuberculosis

Enzymatic activity of Biochemical and Structural Studies of Malate Synthase From Mycobacterium Tuberculosis

All present enzymatic activity of Biochemical and Structural Studies of Malate Synthase From Mycobacterium Tuberculosis:
4.1.3.2;

Protein crystallography data

The structure of Biochemical and Structural Studies of Malate Synthase From Mycobacterium Tuberculosis, PDB code: 1n8i was solved by C.V.Smith, C.C.Huang, A.Miczak, D.G.Russell, J.C.Sacchettini, K.Honer Zu Bentrup, Tb Structural Genomics Consortium (Tbsgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.10
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 78.095, 78.095, 223.180, 90.00, 90.00, 90.00
R / Rfree (%) 18.5 / 23.1

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Biochemical and Structural Studies of Malate Synthase From Mycobacterium Tuberculosis (pdb code 1n8i). 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 Biochemical and Structural Studies of Malate Synthase From Mycobacterium Tuberculosis, PDB code: 1n8i:

Magnesium binding site 1 out of 1 in 1n8i

Go back to Magnesium Binding Sites List in 1n8i
Magnesium binding site 1 out of 1 in the Biochemical and Structural Studies of Malate Synthase 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 Biochemical and Structural Studies of Malate Synthase From Mycobacterium Tuberculosis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg900

b:13.6
occ:1.00
OD1 A:ASP462 2.0 11.2 1.0
O3 A:GLV901 2.1 12.9 1.0
OE2 A:GLU434 2.1 11.1 1.0
O A:HOH1345 2.1 11.8 1.0
O A:HOH1034 2.2 10.7 1.0
O1 A:GLV901 2.4 13.3 1.0
C2 A:GLV901 2.9 13.0 1.0
CG A:ASP462 3.0 11.2 1.0
C1 A:GLV901 3.1 13.0 1.0
CD A:GLU434 3.1 11.2 1.0
CB A:ASP462 3.4 10.8 1.0
OE1 A:GLU434 3.5 11.1 1.0
O A:HOH1312 3.8 30.8 1.0
NH1 A:ARG339 3.9 11.2 1.0
OD1 A:ASP274 4.0 12.6 1.0
NZ A:LYS399 4.1 9.3 1.0
O2 A:GLV901 4.1 12.8 1.0
OD2 A:ASP462 4.1 11.4 1.0
CB A:ALA635 4.3 13.1 1.0
CG A:GLU434 4.4 11.3 1.0
N A:ASP462 4.5 10.5 1.0
OE1 A:GLU273 4.5 9.8 1.0
CA A:ASP462 4.5 10.7 1.0
CB A:GLU434 4.6 11.4 1.0
CE A:MET432 4.8 11.1 1.0
CG A:ASP274 4.9 12.3 1.0
CZ A:ARG339 5.0 10.9 1.0

Reference:

C.V.Smith, C.C.Huang, A.Miczak, D.G.Russell, J.C.Sacchettini, K.Honer Zu Bentrup. Biochemical and Structural Studies of Malate Synthase From Mycobacterium Tuberculosis J.Biol.Chem. V. 278 1735 2003.
ISSN: ISSN 0021-9258
PubMed: 12393860
DOI: 10.1074/JBC.M209248200
Page generated: Tue Aug 13 09:46:37 2024

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