Atomistry » Magnesium » PDB 5d1f-5d9c » 5d6r
Atomistry »
  Magnesium »
    PDB 5d1f-5d9c »
      5d6r »

Magnesium in PDB 5d6r: Acetolactate Synthase From Klebsiella Pneumoniae in Complex with Mechanism-Based Inhibitor

Enzymatic activity of Acetolactate Synthase From Klebsiella Pneumoniae in Complex with Mechanism-Based Inhibitor

All present enzymatic activity of Acetolactate Synthase From Klebsiella Pneumoniae in Complex with Mechanism-Based Inhibitor:
2.2.1.6;

Protein crystallography data

The structure of Acetolactate Synthase From Klebsiella Pneumoniae in Complex with Mechanism-Based Inhibitor, PDB code: 5d6r was solved by A.J.Latta, F.H.Andrews, M.J.Mcleish, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 55.07 / 2.28
Space group I 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 85.120, 133.350, 110.624, 90.00, 95.40, 90.00
R / Rfree (%) 20.1 / 23.6

Other elements in 5d6r:

The structure of Acetolactate Synthase From Klebsiella Pneumoniae in Complex with Mechanism-Based Inhibitor also contains other interesting chemical elements:

Fluorine (F) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Acetolactate Synthase From Klebsiella Pneumoniae in Complex with Mechanism-Based Inhibitor (pdb code 5d6r). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 5 binding sites of Magnesium where determined in the Acetolactate Synthase From Klebsiella Pneumoniae in Complex with Mechanism-Based Inhibitor, PDB code: 5d6r:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5;

Magnesium binding site 1 out of 5 in 5d6r

Go back to Magnesium Binding Sites List in 5d6r
Magnesium binding site 1 out of 5 in the Acetolactate Synthase From Klebsiella Pneumoniae in Complex with Mechanism-Based Inhibitor


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Acetolactate Synthase From Klebsiella Pneumoniae in Complex with Mechanism-Based Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg601

b:39.5
occ:1.00
O23 B:EN0605 2.0 40.2 1.0
O28 B:EN0605 2.2 43.4 1.0
O B:HOH705 2.2 48.3 1.0
OD2 B:ASP474 2.2 59.3 1.0
OD1 B:ASP447 2.2 51.8 1.0
O B:GLY476 2.3 57.9 1.0
CG B:ASP447 3.1 52.3 1.0
P25 B:EN0605 3.1 43.6 1.0
P22 B:EN0605 3.3 40.7 1.0
CG B:ASP474 3.3 60.7 1.0
O27 B:EN0605 3.4 44.5 1.0
OD2 B:ASP447 3.4 53.5 1.0
C B:GLY476 3.5 56.5 1.0
O24 B:EN0605 3.6 46.3 1.0
OD1 B:ASP474 3.8 60.0 1.0
N B:ASP447 3.8 50.8 1.0
N B:GLY476 4.0 60.4 1.0
O21 B:EN0605 4.1 45.4 1.0
N B:GLY448 4.1 51.7 1.0
O B:TRP472 4.2 64.7 1.0
O29 B:EN0605 4.3 40.0 1.0
CA B:GLY476 4.4 59.5 1.0
CB B:ASP447 4.4 51.3 1.0
N B:ASN478 4.5 53.9 1.0
CB B:ASP474 4.5 63.1 1.0
O26 B:EN0605 4.5 42.2 1.0
N B:TYR477 4.5 52.0 1.0
CA B:GLY446 4.5 57.7 1.0
N B:ASP474 4.5 63.1 1.0
CA B:ASP447 4.6 50.3 1.0
C B:GLY446 4.6 58.4 1.0
CA B:TYR477 4.6 50.3 1.0
N B:ASN475 4.8 64.7 1.0
CZ B:PHE496 4.8 54.5 1.0
C B:ASP447 4.9 49.3 1.0
CA B:ASP474 4.9 64.6 1.0
CB B:ASN478 5.0 55.8 1.0

Magnesium binding site 2 out of 5 in 5d6r

Go back to Magnesium Binding Sites List in 5d6r
Magnesium binding site 2 out of 5 in the Acetolactate Synthase From Klebsiella Pneumoniae in Complex with Mechanism-Based Inhibitor


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Acetolactate Synthase From Klebsiella Pneumoniae in Complex with Mechanism-Based Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg602

b:47.0
occ:1.00
O B:SER129 2.6 41.3 1.0
O B:HOH776 2.6 23.2 1.0
O B:THR132 2.9 30.9 1.0
O B:HOH816 3.0 45.4 1.0
C B:SER129 3.6 39.7 1.0
C B:THR132 4.1 31.7 1.0
CA B:SER129 4.3 40.2 1.0
O B:LYS133 4.5 28.0 1.0
CB B:SER129 4.6 39.6 1.0
C B:LYS133 4.7 28.3 1.0
N B:PRO130 4.7 34.0 1.0
O B:HOH752 4.7 36.4 1.0
OG1 B:THR132 4.8 29.1 1.0
N B:THR132 4.8 28.9 1.0
CA B:LYS133 4.9 28.0 1.0
CA B:PRO130 4.9 33.0 1.0
N B:LYS133 4.9 28.9 1.0

Magnesium binding site 3 out of 5 in 5d6r

Go back to Magnesium Binding Sites List in 5d6r
Magnesium binding site 3 out of 5 in the Acetolactate Synthase From Klebsiella Pneumoniae in Complex with Mechanism-Based Inhibitor


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Acetolactate Synthase From Klebsiella Pneumoniae in Complex with Mechanism-Based Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg603

b:55.5
occ:1.00
O B:ARG69 2.3 50.9 1.0
OE1 B:GLN220 2.4 39.7 1.0
O B:HOH747 2.5 34.3 1.0
O B:HOH784 2.5 31.0 1.0
C B:ARG69 3.4 49.9 1.0
O B:HOH809 3.6 39.5 1.0
CD B:PRO221 3.6 40.2 1.0
CD B:GLN220 3.6 37.2 1.0
O B:HOH771 3.7 41.3 1.0
O B:HOH772 3.8 47.1 1.0
CA B:ARG69 4.0 48.4 1.0
O B:GLY68 4.2 46.3 1.0
CG B:PRO221 4.2 39.9 1.0
O B:HOH813 4.2 43.6 1.0
NE2 B:GLN220 4.3 36.1 1.0
O B:ILE70 4.3 49.9 1.0
CA B:GLY72 4.4 41.5 1.0
N B:ILE70 4.4 49.3 1.0
N B:GLY72 4.5 42.7 1.0
C B:ILE70 4.6 48.8 1.0
CA B:GLN220 4.7 38.7 1.0
CG B:ARG69 4.7 47.7 1.0
CA B:ILE70 4.8 49.7 1.0
CB B:GLN220 4.8 37.6 1.0
CG B:GLN220 4.8 36.5 1.0
N B:PRO221 4.9 40.3 1.0
CB B:ARG69 5.0 47.4 1.0

Magnesium binding site 4 out of 5 in 5d6r

Go back to Magnesium Binding Sites List in 5d6r
Magnesium binding site 4 out of 5 in the Acetolactate Synthase From Klebsiella Pneumoniae in Complex with Mechanism-Based Inhibitor


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Acetolactate Synthase From Klebsiella Pneumoniae in Complex with Mechanism-Based Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
M:Mg601

b:34.7
occ:1.00
OD1 M:ASP474 2.0 49.8 1.0
O26 M:EN0604 2.1 36.1 1.0
O M:GLY476 2.1 44.1 1.0
OD1 M:ASP447 2.2 37.2 1.0
O23 M:EN0604 2.3 31.4 1.0
O M:HOH708 2.3 36.8 1.0
CG M:ASP474 3.1 50.3 1.0
CG M:ASP447 3.1 36.9 1.0
P25 M:EN0604 3.2 36.0 1.0
C M:GLY476 3.3 43.4 1.0
OD2 M:ASP447 3.4 37.6 1.0
P22 M:EN0604 3.5 31.5 1.0
OD2 M:ASP474 3.5 50.4 1.0
O28 M:EN0604 3.6 36.5 1.0
O24 M:EN0604 3.7 45.6 1.0
N M:GLY476 3.8 45.6 1.0
N M:ASP447 4.0 36.0 1.0
CA M:GLY476 4.2 43.9 1.0
O21 M:EN0604 4.2 32.2 1.0
N M:GLY448 4.2 37.3 1.0
N M:ASN478 4.3 36.8 1.0
CB M:ASP474 4.3 50.6 1.0
N M:TYR477 4.3 37.0 1.0
O M:TRP472 4.4 41.2 1.0
CB M:ASP447 4.5 35.9 1.0
N M:ASP474 4.5 49.3 1.0
CA M:TYR477 4.5 35.6 1.0
O27 M:EN0604 4.5 35.4 1.0
O29 M:EN0604 4.6 32.3 1.0
N M:ASN475 4.6 45.5 1.0
CZ M:PHE496 4.6 39.0 1.0
CA M:ASP447 4.7 36.1 1.0
CA M:GLY446 4.8 42.4 1.0
CA M:ASP474 4.8 50.3 1.0
C M:GLY446 4.8 41.2 1.0
C M:ASP474 4.9 50.5 1.0
CB M:ASN478 4.9 39.4 1.0
C M:ASN475 4.9 45.7 1.0
C M:TYR477 5.0 35.8 1.0
C M:ASP447 5.0 36.2 1.0

Magnesium binding site 5 out of 5 in 5d6r

Go back to Magnesium Binding Sites List in 5d6r
Magnesium binding site 5 out of 5 in the Acetolactate Synthase From Klebsiella Pneumoniae in Complex with Mechanism-Based Inhibitor


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 5 of Acetolactate Synthase From Klebsiella Pneumoniae in Complex with Mechanism-Based Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
M:Mg602

b:45.2
occ:1.00
O M:SER129 2.4 39.5 1.0
O M:THR132 2.6 35.6 1.0
O M:HOH833 2.7 39.0 1.0
O M:HOH733 2.7 31.4 1.0
C M:SER129 3.5 38.7 1.0
C M:THR132 3.8 35.5 1.0
CA M:SER129 4.1 38.8 1.0
N M:THR132 4.4 33.3 1.0
OG1 M:THR132 4.5 32.2 1.0
N M:PRO130 4.5 36.9 1.0
O M:LYS133 4.6 31.8 1.0
C M:LYS133 4.6 29.5 1.0
CB M:SER129 4.6 41.1 1.0
CA M:THR132 4.7 34.3 1.0
N M:LYS133 4.7 30.2 1.0
CA M:LYS133 4.7 30.0 1.0
CA M:PRO130 4.7 37.2 1.0
C M:PRO130 4.8 38.2 1.0
N M:VAL131 5.0 31.3 1.0

Reference:

A.J.Latta, F.H.Andrews, M.J.Mcleish. Acetolactate Synthase From Klebsiella Pneumoniae in Complex with Mechanism-Based Inhibitor To Be Published.
Page generated: Mon Dec 14 20:10:20 2020

Last articles

Zn in 7VD8
Zn in 7V1R
Zn in 7V1Q
Zn in 7VPF
Zn in 7T85
Zn in 7T5F
Zn in 7NF9
Zn in 7M4M
Zn in 7M4O
Zn in 7M4N
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy