Atomistry » Magnesium » PDB 1ozf-1php » 1ozf
Atomistry »
  Magnesium »
    PDB 1ozf-1php »
      1ozf »

Magnesium in PDB 1ozf: The Crystal Structure of Klebsiella Pneumoniae Acetolactate Synthase with Enzyme-Bound Cofactors

Enzymatic activity of The Crystal Structure of Klebsiella Pneumoniae Acetolactate Synthase with Enzyme-Bound Cofactors

All present enzymatic activity of The Crystal Structure of Klebsiella Pneumoniae Acetolactate Synthase with Enzyme-Bound Cofactors:
4.1.3.18;

Protein crystallography data

The structure of The Crystal Structure of Klebsiella Pneumoniae Acetolactate Synthase with Enzyme-Bound Cofactors, PDB code: 1ozf was solved by S.S.Pang, R.G.Duggleby, R.L.Schowen, L.W.Guddat, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 100.00 / 2.30
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 116.822, 160.573, 129.374, 90.00, 90.00, 90.00
R / Rfree (%) 16.5 / 21.4

Magnesium Binding Sites:

The binding sites of Magnesium atom in the The Crystal Structure of Klebsiella Pneumoniae Acetolactate Synthase with Enzyme-Bound Cofactors (pdb code 1ozf). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the The Crystal Structure of Klebsiella Pneumoniae Acetolactate Synthase with Enzyme-Bound Cofactors, PDB code: 1ozf:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 1ozf

Go back to Magnesium Binding Sites List in 1ozf
Magnesium binding site 1 out of 2 in the The Crystal Structure of Klebsiella Pneumoniae Acetolactate Synthase with Enzyme-Bound Cofactors


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of The Crystal Structure of Klebsiella Pneumoniae Acetolactate Synthase with Enzyme-Bound Cofactors within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg699

b:12.6
occ:1.00
O3B A:TPP700 2.0 8.4 1.0
OD1 A:ASP474 2.1 18.5 1.0
O A:GLY476 2.1 16.3 1.0
O A:HOH740 2.1 9.4 1.0
O1A A:TPP700 2.2 8.4 1.0
OD1 A:ASP447 2.3 14.9 1.0
PB A:TPP700 3.0 11.2 1.0
CG A:ASP474 3.1 17.4 1.0
PA A:TPP700 3.1 13.5 1.0
O3A A:TPP700 3.3 11.3 1.0
C A:GLY476 3.3 16.0 1.0
OD2 A:ASP474 3.5 18.1 1.0
CG A:ASP447 3.5 14.9 1.0
O1B A:TPP700 3.5 8.2 1.0
O7 A:TPP700 3.7 14.7 1.0
N A:ASP447 3.9 11.5 1.0
OD2 A:ASP447 4.0 15.4 1.0
N A:GLY476 4.0 16.0 1.0
N A:ASN478 4.0 13.9 1.0
N A:TYR477 4.2 14.6 1.0
CA A:GLY476 4.2 16.4 1.0
N A:GLY448 4.3 10.2 1.0
CA A:TYR477 4.3 14.6 1.0
O2B A:TPP700 4.4 7.6 1.0
CB A:ASP474 4.4 14.5 1.0
O2A A:TPP700 4.5 12.2 1.0
O A:TRP472 4.5 9.8 1.0
CA A:GLY446 4.5 10.4 1.0
N A:ASP474 4.6 12.8 1.0
C A:GLY446 4.6 10.7 1.0
CZ A:PHE496 4.6 10.6 1.0
CB A:ASP447 4.7 11.9 1.0
C A:TYR477 4.7 15.3 1.0
CA A:ASP447 4.7 12.3 1.0
CB A:ASN478 4.8 13.1 1.0
C7 A:TPP700 4.8 16.4 1.0
N A:ASN475 4.9 14.6 1.0
CA A:ASP474 5.0 13.8 1.0

Magnesium binding site 2 out of 2 in 1ozf

Go back to Magnesium Binding Sites List in 1ozf
Magnesium binding site 2 out of 2 in the The Crystal Structure of Klebsiella Pneumoniae Acetolactate Synthase with Enzyme-Bound Cofactors


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of The Crystal Structure of Klebsiella Pneumoniae Acetolactate Synthase with Enzyme-Bound Cofactors within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg704

b:15.2
occ:1.00
O3B B:TPP705 2.0 14.8 1.0
O B:HOH706 2.1 15.7 1.0
OD1 B:ASP474 2.1 17.1 1.0
O1A B:TPP705 2.1 16.3 1.0
O B:GLY476 2.2 15.9 1.0
OD1 B:ASP447 2.3 16.1 1.0
CG B:ASP474 3.0 17.5 1.0
PB B:TPP705 3.0 14.4 1.0
PA B:TPP705 3.1 15.1 1.0
O3A B:TPP705 3.2 15.7 1.0
C B:GLY476 3.4 16.2 1.0
OD2 B:ASP474 3.4 18.9 1.0
CG B:ASP447 3.4 16.1 1.0
O1B B:TPP705 3.5 14.8 1.0
O7 B:TPP705 3.7 18.4 1.0
N B:ASP447 3.9 12.8 1.0
OD2 B:ASP447 4.0 15.3 1.0
N B:GLY476 4.0 17.9 1.0
N B:ASN478 4.1 15.9 1.0
N B:TYR477 4.3 17.0 1.0
N B:GLY448 4.3 12.8 1.0
CB B:ASP474 4.3 18.0 1.0
CA B:GLY476 4.3 16.8 1.0
CA B:TYR477 4.3 16.5 1.0
O2B B:TPP705 4.4 14.6 1.0
O2A B:TPP705 4.4 18.0 1.0
CA B:GLY446 4.5 14.1 1.0
O B:TRP472 4.5 14.3 1.0
C B:GLY446 4.6 13.5 1.0
N B:ASP474 4.6 14.8 1.0
CB B:ASP447 4.6 13.8 1.0
CZ B:PHE496 4.7 19.6 1.0
CA B:ASP447 4.7 14.7 1.0
C7 B:TPP705 4.8 21.4 1.0
CB B:ASN478 4.8 14.5 1.0
C B:TYR477 4.8 15.3 1.0
N B:ASN475 4.8 16.4 1.0
CE1 B:TYR543 4.9 14.2 1.0
CA B:ASP474 4.9 15.8 1.0

Reference:

S.S.Pang, R.G.Duggleby, R.L.Schowen, L.W.Guddat. The Crystal Structures of Klebsiella Pneumoniae Acetolactate Synthase with Enzyme-Bound Cofactor and with An Unusual Intermediate. J.Biol.Chem. V. 279 2242 2004.
ISSN: ISSN 0021-9258
PubMed: 14557277
DOI: 10.1074/JBC.M304038200
Page generated: Mon Dec 14 06:35:30 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