Atomistry » Magnesium » PDB 1xfy-1xon » 1xg4
Atomistry »
  Magnesium »
    PDB 1xfy-1xon »
      1xg4 »

Magnesium in PDB 1xg4: Crystal Structure of the C123S 2-Methylisocitrate Lyase Mutant From Escherichia Coli in Complex with the Inhibitor Isocitrate

Enzymatic activity of Crystal Structure of the C123S 2-Methylisocitrate Lyase Mutant From Escherichia Coli in Complex with the Inhibitor Isocitrate

All present enzymatic activity of Crystal Structure of the C123S 2-Methylisocitrate Lyase Mutant From Escherichia Coli in Complex with the Inhibitor Isocitrate:
4.1.3.30;

Protein crystallography data

The structure of Crystal Structure of the C123S 2-Methylisocitrate Lyase Mutant From Escherichia Coli in Complex with the Inhibitor Isocitrate, PDB code: 1xg4 was solved by S.Liu, Z.Lu, Y.Han, E.Melamud, D.Dunaway-Mariano, O.Herzberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.29 / 1.60
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 159.061, 84.561, 99.756, 90.00, 108.15, 90.00
R / Rfree (%) 18.1 / 20.1

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the C123S 2-Methylisocitrate Lyase Mutant From Escherichia Coli in Complex with the Inhibitor Isocitrate (pdb code 1xg4). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Crystal Structure of the C123S 2-Methylisocitrate Lyase Mutant From Escherichia Coli in Complex with the Inhibitor Isocitrate, PDB code: 1xg4:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in 1xg4

Go back to Magnesium Binding Sites List in 1xg4
Magnesium binding site 1 out of 3 in the Crystal Structure of the C123S 2-Methylisocitrate Lyase Mutant From Escherichia Coli in Complex with the Inhibitor Isocitrate


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 the C123S 2-Methylisocitrate Lyase Mutant From Escherichia Coli in Complex with the Inhibitor Isocitrate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1101

b:26.1
occ:1.00
O A:HOH1360 2.1 21.0 1.0
OD2 A:ASP85 2.2 18.4 1.0
O A:HOH1361 2.4 23.4 1.0
O2 A:ICT1105 2.4 24.0 1.0
O A:HOH1362 2.4 23.9 1.0
O7 A:ICT1105 2.6 29.0 1.0
C1 A:ICT1105 3.3 27.6 1.0
CG A:ASP85 3.3 16.8 1.0
C2 A:ICT1105 3.4 26.9 1.0
OD1 A:ASP85 3.7 18.0 1.0
NZ A:LYS121 3.8 27.6 1.0
N A:GLY47 3.9 15.4 1.0
OD2 A:ASP58 3.9 20.2 1.0
OD1 A:ASP87 4.0 30.5 1.0
NH1 A:ARG158 4.1 21.5 1.0
C3 A:ICT1105 4.1 25.7 1.0
O6 A:ICT1105 4.1 23.5 1.0
N A:GLY46 4.1 12.8 1.0
CA A:GLY46 4.2 14.9 1.0
OD1 A:ASP58 4.3 20.5 1.0
C A:GLY46 4.4 15.3 1.0
O1 A:ICT1105 4.4 29.2 1.0
CG A:ASP58 4.5 20.7 1.0
CB A:ASP85 4.5 16.8 1.0
C6 A:ICT1105 4.6 25.0 1.0
CA A:GLY47 4.7 15.1 1.0
CE A:LYS121 4.8 26.9 1.0
OH A:TYR43 4.9 16.7 1.0
OE1 A:GLU115 4.9 25.2 1.0

Magnesium binding site 2 out of 3 in 1xg4

Go back to Magnesium Binding Sites List in 1xg4
Magnesium binding site 2 out of 3 in the Crystal Structure of the C123S 2-Methylisocitrate Lyase Mutant From Escherichia Coli in Complex with the Inhibitor Isocitrate


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 the C123S 2-Methylisocitrate Lyase Mutant From Escherichia Coli in Complex with the Inhibitor Isocitrate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg1201

b:28.6
occ:1.00
OD2 B:ASP85 2.0 21.9 1.0
O B:HOH1467 2.3 24.2 1.0
O B:HOH1465 2.3 22.7 1.0
O2 B:ICT1205 2.4 27.4 1.0
O B:HOH1466 2.5 29.2 1.0
O7 B:ICT1205 2.7 29.6 1.0
CG B:ASP85 3.1 19.6 1.0
C1 B:ICT1205 3.2 28.4 1.0
C2 B:ICT1205 3.4 26.6 1.0
OD1 B:ASP85 3.7 20.6 1.0
N B:GLY47 3.9 15.6 1.0
NZ B:LYS121 4.0 29.1 1.0
OD2 B:ASP58 4.0 19.4 1.0
N B:GLY46 4.0 14.8 1.0
CA B:GLY46 4.0 16.1 1.0
OD1 B:ASP87 4.0 27.9 1.0
C3 B:ICT1205 4.1 26.4 1.0
NH1 B:ARG158 4.2 20.3 1.0
O6 B:ICT1205 4.3 24.1 1.0
O1 B:ICT1205 4.3 30.5 1.0
C B:GLY46 4.3 16.0 1.0
CB B:ASP85 4.3 18.7 1.0
OD1 B:ASP58 4.5 20.6 1.0
C6 B:ICT1205 4.6 24.6 1.0
CG B:ASP58 4.6 20.9 1.0
OH B:TYR43 4.7 17.9 1.0
CA B:GLY47 4.8 15.5 1.0
OE1 B:GLU115 4.9 24.6 1.0
CE1 B:HIS113 4.9 18.2 1.0
CE B:LYS121 5.0 27.7 1.0

Magnesium binding site 3 out of 3 in 1xg4

Go back to Magnesium Binding Sites List in 1xg4
Magnesium binding site 3 out of 3 in the Crystal Structure of the C123S 2-Methylisocitrate Lyase Mutant From Escherichia Coli in Complex with the Inhibitor Isocitrate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of the C123S 2-Methylisocitrate Lyase Mutant From Escherichia Coli in Complex with the Inhibitor Isocitrate within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg1401

b:25.2
occ:1.00
OD2 D:ASP85 2.1 22.4 1.0
O D:HOH1633 2.3 20.5 1.0
O D:HOH1635 2.3 21.7 1.0
O D:HOH1634 2.4 21.6 1.0
O2 D:ICT1405 2.4 27.7 1.0
O7 D:ICT1405 2.6 28.8 1.0
CG D:ASP85 3.2 20.1 1.0
C1 D:ICT1405 3.2 27.6 1.0
C2 D:ICT1405 3.4 26.1 1.0
OD1 D:ASP85 3.6 18.8 1.0
NZ D:LYS121 3.9 24.4 1.0
OD2 D:ASP58 3.9 21.7 1.0
N D:GLY47 3.9 14.1 1.0
OD2 D:ASP87 3.9 30.4 1.0
NH1 D:ARG158 4.1 24.6 1.0
C3 D:ICT1405 4.1 25.1 1.0
N D:GLY46 4.1 14.6 1.0
CA D:GLY46 4.1 14.2 1.0
O6 D:ICT1405 4.2 23.1 1.0
O1 D:ICT1405 4.3 28.3 1.0
C D:GLY46 4.4 13.9 1.0
CB D:ASP85 4.4 17.8 1.0
OD1 D:ASP58 4.5 20.0 1.0
C6 D:ICT1405 4.6 24.7 1.0
CG D:ASP58 4.6 22.0 1.0
CA D:GLY47 4.8 15.1 1.0
OH D:TYR43 4.8 19.0 1.0
CE D:LYS121 4.8 23.1 1.0
OE1 D:GLU115 4.9 25.8 1.0
CE1 D:HIS113 5.0 17.7 1.0

Reference:

S.Liu, Z.Lu, Y.Han, E.Melamud, D.Dunaway-Mariano, O.Herzberg. Crystal Structures of 2-Methylisocitrate Lyase in Complex with Product and with Isocitrate Inhibitor Provide Insight Into Lyase Substrate Specificity, Catalysis and Evolution Biochemistry V. 44 2949 2005.
ISSN: ISSN 0006-2960
PubMed: 15723538
DOI: 10.1021/BI0479712
Page generated: Mon Dec 14 07:04:11 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy