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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

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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: Sun Sep 29 02:33:00 2024

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