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Magnesium in PDB 1ozg: The Crystal Structure of Klebsiella Pneumoniae Acetolactate Synthase with Enzyme-Bound Cofactor and with An Unusual Intermediate

Enzymatic activity of The Crystal Structure of Klebsiella Pneumoniae Acetolactate Synthase with Enzyme-Bound Cofactor and with An Unusual Intermediate

All present enzymatic activity of The Crystal Structure of Klebsiella Pneumoniae Acetolactate Synthase with Enzyme-Bound Cofactor and with An Unusual Intermediate:
4.1.3.18;

Protein crystallography data

The structure of The Crystal Structure of Klebsiella Pneumoniae Acetolactate Synthase with Enzyme-Bound Cofactor and with An Unusual Intermediate, PDB code: 1ozg 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 (°) 117.488, 160.561, 129.454, 90.00, 90.00, 90.00
R / Rfree (%) 16.2 / 21.4

Magnesium Binding Sites:

The binding sites of Magnesium atom in the The Crystal Structure of Klebsiella Pneumoniae Acetolactate Synthase with Enzyme-Bound Cofactor and with An Unusual Intermediate (pdb code 1ozg). 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 Cofactor and with An Unusual Intermediate, PDB code: 1ozg:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 1ozg

Go back to Magnesium Binding Sites List in 1ozg
Magnesium binding site 1 out of 2 in the The Crystal Structure of Klebsiella Pneumoniae Acetolactate Synthase with Enzyme-Bound Cofactor and with An Unusual Intermediate


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 Cofactor and with An Unusual Intermediate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg699

b:14.6
occ:1.00
O3B A:HE3700 1.9 8.6 1.0
O A:GLY476 2.0 15.7 1.0
O2A A:HE3700 2.0 10.2 1.0
O A:HOH740 2.1 13.0 1.0
OD1 A:ASP474 2.2 17.4 1.0
OD1 A:ASP447 2.3 17.2 1.0
PB A:HE3700 3.0 13.9 1.0
PA A:HE3700 3.1 14.8 1.0
CG A:ASP474 3.1 18.3 1.0
O1A A:HE3700 3.2 15.0 1.0
C A:GLY476 3.3 16.0 1.0
CG A:ASP447 3.5 16.8 1.0
O1B A:HE3700 3.5 9.2 1.0
OD2 A:ASP474 3.5 16.7 1.0
O7 A:HE3700 3.6 14.8 1.0
N A:ASP447 3.9 12.5 1.0
N A:GLY476 4.0 16.5 1.0
N A:ASN478 4.0 15.8 1.0
OD2 A:ASP447 4.0 16.5 1.0
N A:TYR477 4.2 15.7 1.0
N A:GLY448 4.2 10.0 1.0
CA A:GLY476 4.2 15.6 1.0
CA A:TYR477 4.3 15.3 1.0
O2B A:HE3700 4.3 11.6 1.0
CB A:ASP474 4.4 12.0 1.0
O3A A:HE3700 4.4 14.2 1.0
CA A:GLY446 4.6 11.8 1.0
CB A:ASP447 4.6 13.8 1.0
O A:TRP472 4.7 11.4 1.0
N A:ASP474 4.7 13.6 1.0
C A:TYR477 4.7 16.7 1.0
C A:GLY446 4.7 11.2 1.0
CB A:ASN478 4.7 14.0 1.0
CA A:ASP447 4.7 12.4 1.0
CZ A:PHE496 4.8 13.1 1.0
N A:ASN475 4.8 16.1 1.0
C7 A:HE3700 4.9 16.4 1.0
C A:ASP447 5.0 12.5 1.0
CA A:ASN478 5.0 15.7 1.0
CA A:ASP474 5.0 13.4 1.0

Magnesium binding site 2 out of 2 in 1ozg

Go back to Magnesium Binding Sites List in 1ozg
Magnesium binding site 2 out of 2 in the The Crystal Structure of Klebsiella Pneumoniae Acetolactate Synthase with Enzyme-Bound Cofactor and with An Unusual Intermediate


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 Cofactor and with An Unusual Intermediate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg704

b:11.0
occ:1.00
OD1 B:ASP474 2.0 18.8 1.0
O3B B:HE3705 2.0 8.1 1.0
O B:HOH706 2.1 24.6 1.0
O2A B:HE3705 2.1 14.9 1.0
O B:GLY476 2.1 14.0 1.0
OD1 B:ASP447 2.2 13.2 1.0
CG B:ASP474 2.9 21.2 1.0
PB B:HE3705 3.1 12.8 1.0
PA B:HE3705 3.1 15.2 1.0
O1A B:HE3705 3.3 14.8 1.0
OD2 B:ASP474 3.3 22.9 1.0
C B:GLY476 3.3 16.7 1.0
CG B:ASP447 3.3 15.8 1.0
O1B B:HE3705 3.6 13.9 1.0
O7 B:HE3705 3.7 14.6 1.0
N B:ASP447 3.8 12.2 1.0
OD2 B:ASP447 3.9 14.5 1.0
N B:GLY476 4.0 16.3 1.0
N B:ASN478 4.2 17.8 1.0
N B:TYR477 4.2 17.6 1.0
CB B:ASP474 4.2 19.5 1.0
N B:GLY448 4.2 14.0 1.0
CA B:GLY476 4.3 17.1 1.0
CA B:TYR477 4.3 17.0 1.0
O2B B:HE3705 4.4 10.8 1.0
O3A B:HE3705 4.4 17.0 1.0
O B:TRP472 4.5 13.0 1.0
CA B:GLY446 4.5 14.5 1.0
CB B:ASP447 4.5 12.4 1.0
CZ B:PHE496 4.5 16.8 1.0
N B:ASP474 4.5 16.4 1.0
C B:GLY446 4.6 12.9 1.0
CA B:ASP447 4.6 14.3 1.0
N B:ASN475 4.8 17.1 1.0
C B:TYR477 4.8 18.2 1.0
CA B:ASP474 4.9 18.4 1.0
C B:ASP447 4.9 14.2 1.0
CB B:ASN478 4.9 16.0 1.0
C7 B:HE3705 5.0 14.2 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: Tue Aug 13 10:46:13 2024

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