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Magnesium in PDB 5oas: Crystal Structure of Malate Synthase G From Pseudomonas Aeruginosa in Apo Form.

Enzymatic activity of Crystal Structure of Malate Synthase G From Pseudomonas Aeruginosa in Apo Form.

All present enzymatic activity of Crystal Structure of Malate Synthase G From Pseudomonas Aeruginosa in Apo Form.:
2.3.3.9;

Protein crystallography data

The structure of Crystal Structure of Malate Synthase G From Pseudomonas Aeruginosa in Apo Form., PDB code: 5oas was solved by A.C.Mcvey, M.Welch, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 69.93 / 1.62
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 71.171, 81.197, 137.574, 90.00, 90.00, 90.00
R / Rfree (%) 16.7 / 19.3

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Malate Synthase G From Pseudomonas Aeruginosa in Apo Form. (pdb code 5oas). 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 Malate Synthase G From Pseudomonas Aeruginosa in Apo Form., PDB code: 5oas:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 5oas

Go back to Magnesium Binding Sites List in 5oas
Magnesium binding site 1 out of 2 in the Crystal Structure of Malate Synthase G From Pseudomonas Aeruginosa in Apo Form.


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 Malate Synthase G From Pseudomonas Aeruginosa in Apo Form. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg820

b:36.5
occ:1.00
OE2 A:GLU432 2.7 18.4 1.0
OE1 A:GLU274 2.8 19.5 1.0
OD2 A:ASP460 3.1 26.5 1.0
OE1 A:GLU432 3.2 26.1 1.0
CD A:GLU432 3.3 21.1 1.0
NH1 A:ARG340 3.3 21.7 1.0
O2 A:EDO808 3.3 45.5 1.0
NZ A:LYS397 3.3 21.2 1.0
OE2 A:GLU274 3.4 19.1 1.0
CB A:PRO396 3.4 15.3 1.0
CD A:GLU274 3.5 19.8 1.0
O A:HOH969 3.6 40.9 1.0
OD2 A:ASP275 3.9 27.4 1.0
CZ A:ARG340 4.0 15.7 1.0
CG A:ASP275 4.2 22.9 1.0
CG A:LYS397 4.3 17.7 1.0
CG A:ASP460 4.4 23.7 1.0
C2 A:EDO808 4.4 41.9 1.0
CG A:PRO396 4.5 15.6 1.0
CA A:PRO396 4.6 14.3 1.0
CE A:LYS397 4.6 19.9 1.0
NH2 A:ARG340 4.6 17.3 1.0
NE A:ARG340 4.6 14.4 1.0
OD1 A:ASP275 4.6 22.0 1.0
CD A:ARG340 4.7 15.0 1.0
CG A:GLU432 4.7 15.5 1.0
CB A:ASP275 4.7 18.7 1.0
CG A:MET430 4.7 16.4 1.0
CD A:LYS397 4.8 18.4 1.0
N A:LYS397 4.8 15.5 1.0
CG A:GLU274 5.0 18.3 1.0

Magnesium binding site 2 out of 2 in 5oas

Go back to Magnesium Binding Sites List in 5oas
Magnesium binding site 2 out of 2 in the Crystal Structure of Malate Synthase G From Pseudomonas Aeruginosa in Apo Form.


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 Malate Synthase G From Pseudomonas Aeruginosa in Apo Form. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg821

b:36.9
occ:1.00
C2 A:GOL803 2.7 40.6 1.0
C3 A:GOL803 2.9 35.6 1.0
OD1 A:ASP318 2.9 17.3 1.0
N A:ARG334 2.9 14.7 1.0
N A:GLY333 3.0 15.8 1.0
CB A:HIS332 3.3 17.9 1.0
O2 A:GOL803 3.3 46.9 1.0
CZ A:ARG334 3.3 21.5 1.0
NH2 A:ARG334 3.4 18.9 1.0
CA A:HIS332 3.4 17.1 1.0
C A:HIS332 3.4 15.2 1.0
NH2 A:ARG387 3.5 35.3 1.0
CB A:ARG334 3.5 14.3 1.0
NH1 A:ARG334 3.5 19.1 1.0
CA A:ARG334 3.7 13.6 1.0
O A:ARG334 3.7 15.3 1.0
C A:GLY333 3.8 14.6 1.0
CA A:GLY333 3.8 16.9 1.0
NE A:ARG334 3.8 15.3 1.0
C1 A:GOL803 3.9 39.1 1.0
CG A:HIS332 4.0 25.9 1.0
CG A:ARG334 4.0 17.3 1.0
CG A:ASP318 4.0 21.0 1.0
O3 A:GOL803 4.1 38.1 1.0
C A:ARG334 4.1 13.8 1.0
O A:HIS332 4.4 15.4 1.0
CD2 A:HIS332 4.5 30.4 1.0
OD2 A:ASP318 4.6 22.8 1.0
CD A:ARG334 4.6 16.3 1.0
O A:HOH915 4.7 27.1 1.0
CZ A:ARG387 4.7 35.4 1.0
O A:LYS384 4.8 15.7 1.0
ND1 A:HIS332 4.8 29.0 1.0
N A:HIS332 4.9 16.6 1.0
O1 A:GOL803 4.9 41.4 1.0
O A:GLY333 5.0 15.0 1.0

Reference:

A.C.Mcvey, P.Medarametla, X.Chee, S.Bartlett, A.Poso, D.R.Spring, T.Rahman, M.Welch. Structural and Functional Characterization of Malate Synthase G From Opportunistic Pathogen Pseudomonas Aeruginosa. Biochemistry V. 56 5539 2017.
ISSN: ISSN 1520-4995
PubMed: 28985053
DOI: 10.1021/ACS.BIOCHEM.7B00852
Page generated: Mon Sep 30 00:14:01 2024

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