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Magnesium in PDB 1ozh: 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: 1ozh 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 / 2.00
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 86.320, 92.814, 97.420, 67.97, 63.48, 67.68
R / Rfree (%) 19.1 / 22.8

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 1ozh). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 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: 1ozh:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 1ozh

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Magnesium binding site 1 out of 4 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:Mg1405

b:22.9
occ:1.00
OD1 A:ASP474 1.9 26.7 1.0
O A:GLY476 2.0 25.0 1.0
O3B A:HE31406 2.1 20.7 1.0
O2A A:HE31406 2.1 19.9 1.0
O A:HOH1435 2.2 25.6 1.0
OD1 A:ASP447 2.2 23.8 1.0
CG A:ASP474 2.8 26.6 1.0
PB A:HE31406 3.2 21.6 1.0
OD2 A:ASP474 3.2 26.4 1.0
PA A:HE31406 3.2 23.0 1.0
C A:GLY476 3.2 21.7 1.0
CG A:ASP447 3.3 22.1 1.0
O1A A:HE31406 3.4 22.9 1.0
O1B A:HE31406 3.6 22.3 1.0
N A:GLY476 3.7 23.8 1.0
O7 A:HE31406 3.8 20.3 1.0
OD2 A:ASP447 3.8 22.8 1.0
N A:ASP447 3.9 18.3 1.0
CA A:GLY476 4.0 23.1 1.0
CB A:ASP474 4.1 26.1 1.0
N A:ASN478 4.2 24.0 1.0
N A:TYR477 4.2 21.8 1.0
N A:GLY448 4.3 19.6 1.0
CA A:TYR477 4.4 22.2 1.0
O2B A:HE31406 4.4 21.3 1.0
N A:ASP474 4.5 25.8 1.0
CZ A:PHE496 4.5 26.2 1.0
O3A A:HE31406 4.5 21.3 1.0
N A:ASN475 4.5 26.4 1.0
CB A:ASP447 4.6 20.2 1.0
O A:TRP472 4.6 25.9 1.0
CA A:GLY446 4.7 20.0 1.0
CA A:ASP447 4.7 18.3 1.0
C A:GLY446 4.7 21.1 1.0
CA A:ASP474 4.8 26.4 1.0
CB A:ASN478 4.8 25.7 1.0
C A:ASP474 4.8 26.4 1.0
C A:TYR477 4.8 22.4 1.0
C A:ASN475 4.9 25.7 1.0
CE1 A:TYR543 5.0 24.8 1.0

Magnesium binding site 2 out of 4 in 1ozh

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Magnesium binding site 2 out of 4 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:Mg1412

b:21.9
occ:1.00
OD1 B:ASP474 2.0 24.4 1.0
O B:GLY476 2.0 17.6 1.0
O2A B:HE31413 2.1 19.3 1.0
O3B B:HE31413 2.1 18.1 1.0
OD1 B:ASP447 2.2 18.6 1.0
O B:HOH1453 2.2 19.9 1.0
CG B:ASP474 3.0 25.2 1.0
PA B:HE31413 3.2 20.6 1.0
PB B:HE31413 3.2 18.8 1.0
C B:GLY476 3.2 20.6 1.0
CG B:ASP447 3.3 21.3 1.0
O1A B:HE31413 3.4 18.4 1.0
OD2 B:ASP474 3.4 22.1 1.0
O1B B:HE31413 3.7 15.9 1.0
O7 B:HE31413 3.7 19.9 1.0
N B:ASP447 3.8 18.0 1.0
OD2 B:ASP447 3.8 22.0 1.0
N B:GLY476 3.8 20.6 1.0
CA B:GLY476 4.1 20.2 1.0
N B:GLY448 4.2 18.9 1.0
N B:ASN478 4.2 21.8 1.0
N B:TYR477 4.2 19.6 1.0
CB B:ASP474 4.3 22.0 1.0
CA B:TYR477 4.4 19.6 1.0
O3A B:HE31413 4.5 19.4 1.0
CB B:ASP447 4.5 18.9 1.0
O2B B:HE31413 4.5 16.4 1.0
O B:TRP472 4.5 19.0 1.0
CA B:GLY446 4.5 18.8 1.0
N B:ASP474 4.5 21.6 1.0
CA B:ASP447 4.6 18.0 1.0
C B:GLY446 4.6 19.8 1.0
CZ B:PHE496 4.6 23.8 1.0
N B:ASN475 4.7 22.1 1.0
C B:TYR477 4.9 21.8 1.0
CA B:ASP474 4.9 23.2 1.0
C B:ASP447 4.9 19.3 1.0
CB B:ASN478 4.9 21.2 1.0
C B:ASP474 5.0 22.0 1.0

Magnesium binding site 3 out of 4 in 1ozh

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Magnesium binding site 3 out of 4 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 3 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
C:Mg1422

b:19.7
occ:1.00
OD1 C:ASP474 2.0 19.4 1.0
O C:GLY476 2.0 20.2 1.0
O C:HOH1451 2.1 18.7 1.0
O2A C:HE31423 2.1 18.5 1.0
O3B C:HE31423 2.1 17.5 1.0
OD1 C:ASP447 2.2 21.2 1.0
CG C:ASP474 3.1 23.6 1.0
PB C:HE31423 3.2 20.0 1.0
PA C:HE31423 3.2 20.9 1.0
C C:GLY476 3.2 20.2 1.0
CG C:ASP447 3.3 23.2 1.0
O1A C:HE31423 3.3 17.3 1.0
OD2 C:ASP474 3.6 21.9 1.0
O1B C:HE31423 3.6 20.1 1.0
O7 C:HE31423 3.7 20.8 1.0
OD2 C:ASP447 3.8 23.4 1.0
N C:GLY476 3.8 21.5 1.0
N C:ASP447 3.8 18.6 1.0
CA C:GLY476 4.1 21.4 1.0
N C:GLY448 4.1 20.7 1.0
N C:ASN478 4.2 20.3 1.0
N C:TYR477 4.2 19.7 1.0
CB C:ASP474 4.3 20.6 1.0
CA C:TYR477 4.3 19.2 1.0
N C:ASP474 4.5 19.2 1.0
O2B C:HE31423 4.5 20.5 1.0
O3A C:HE31423 4.5 17.4 1.0
CB C:ASP447 4.5 20.1 1.0
O C:TRP472 4.5 21.8 1.0
CA C:GLY446 4.6 18.6 1.0
CA C:ASP447 4.6 18.5 1.0
CZ C:PHE496 4.6 22.4 1.0
C C:GLY446 4.6 18.6 1.0
N C:ASN475 4.7 21.4 1.0
C C:TYR477 4.8 19.7 1.0
CA C:ASP474 4.8 20.6 1.0
C C:ASP447 4.9 19.6 1.0
CB C:ASN478 5.0 18.4 1.0
C C:ASP474 5.0 21.0 1.0

Magnesium binding site 4 out of 4 in 1ozh

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Magnesium binding site 4 out of 4 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 4 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
D:Mg1432

b:32.1
occ:1.00
OD1 D:ASP474 2.0 30.8 1.0
O D:GLY476 2.0 26.2 1.0
OD1 D:ASP447 2.1 23.9 1.0
O3B D:HE31433 2.1 25.0 1.0
O2A D:HE31433 2.1 27.0 1.0
O D:HOH1473 2.2 28.7 1.0
CG D:ASP474 3.0 31.3 1.0
PB D:HE31433 3.1 25.2 1.0
PA D:HE31433 3.1 25.1 1.0
CG D:ASP447 3.2 25.7 1.0
C D:GLY476 3.2 26.6 1.0
OD2 D:ASP474 3.3 31.4 1.0
O1A D:HE31433 3.3 27.2 1.0
O1B D:HE31433 3.6 26.6 1.0
O7 D:HE31433 3.7 23.5 1.0
OD2 D:ASP447 3.7 26.6 1.0
N D:ASP447 3.8 24.0 1.0
N D:GLY476 3.9 26.5 1.0
CA D:GLY476 4.1 26.4 1.0
N D:ASN478 4.2 29.1 1.0
N D:TYR477 4.2 25.4 1.0
N D:GLY448 4.2 24.7 1.0
CB D:ASP474 4.3 28.2 1.0
CA D:TYR477 4.3 25.6 1.0
O2B D:HE31433 4.4 26.9 1.0
CB D:ASP447 4.4 23.7 1.0
O3A D:HE31433 4.5 26.0 1.0
CZ D:PHE496 4.5 25.0 1.0
CA D:GLY446 4.5 24.4 1.0
O D:TRP472 4.5 26.5 1.0
CA D:ASP447 4.6 24.5 1.0
C D:GLY446 4.6 23.0 1.0
N D:ASP474 4.6 27.3 1.0
N D:ASN475 4.7 28.4 1.0
C D:TYR477 4.8 27.4 1.0
CA D:ASP474 4.9 28.2 1.0
C D:ASP447 4.9 24.4 1.0
CB D:ASN478 4.9 30.7 1.0
C7 D:HE31433 4.9 27.3 1.0
C D:ASP474 5.0 28.3 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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