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Magnesium in PDB 1oxh: The Crystal Structure of Beta-Ketoacyl-[Acyl Carrier Protein] Synthase II From Streptococcus Pneumoniae, Triclinic Form

Enzymatic activity of The Crystal Structure of Beta-Ketoacyl-[Acyl Carrier Protein] Synthase II From Streptococcus Pneumoniae, Triclinic Form

All present enzymatic activity of The Crystal Structure of Beta-Ketoacyl-[Acyl Carrier Protein] Synthase II From Streptococcus Pneumoniae, Triclinic Form:
2.3.1.41;

Protein crystallography data

The structure of The Crystal Structure of Beta-Ketoacyl-[Acyl Carrier Protein] Synthase II From Streptococcus Pneumoniae, Triclinic Form, PDB code: 1oxh was solved by A.C.Price, C.O.Rock, S.W.White, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.19 / 2.09
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 61.520, 71.646, 96.100, 89.83, 83.09, 69.15
R / Rfree (%) 20.8 / 23.5

Magnesium Binding Sites:

The binding sites of Magnesium atom in the The Crystal Structure of Beta-Ketoacyl-[Acyl Carrier Protein] Synthase II From Streptococcus Pneumoniae, Triclinic Form (pdb code 1oxh). 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 Beta-Ketoacyl-[Acyl Carrier Protein] Synthase II From Streptococcus Pneumoniae, Triclinic Form, PDB code: 1oxh:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 1oxh

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Magnesium binding site 1 out of 4 in the The Crystal Structure of Beta-Ketoacyl-[Acyl Carrier Protein] Synthase II From Streptococcus Pneumoniae, Triclinic Form


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 Beta-Ketoacyl-[Acyl Carrier Protein] Synthase II From Streptococcus Pneumoniae, Triclinic Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg901

b:22.4
occ:1.00
 OE1 A:GLU346 2.4 35.0 1.0
OD1 A:ASN301 2.7 32.4 1.0
O A:ASN392 2.7 39.4 1.0
O A:ASN301 2.7 32.9 1.0
OG A:SER391 2.8 36.5 1.0
O A:ALA302 3.1 35.1 1.0
CD A:GLU346 3.4 36.2 1.0
C A:ALA302 3.5 35.1 1.0
N A:ASN392 3.5 37.5 1.0
C A:ASN301 3.5 32.5 1.0
C A:ASN392 3.6 38.9 1.0
CG A:ASN301 3.7 30.0 1.0
CB A:GLU346 3.7 35.4 1.0
N A:HIS303 3.8 35.7 1.0
CG A:GLU346 3.9 35.1 1.0
CB A:SER391 4.0 35.9 1.0
C A:SER391 4.0 36.4 1.0
O A:HOH925 4.0 36.3 1.0
CB A:ASN301 4.1 29.9 1.0
CA A:ASN392 4.1 38.2 1.0
CA A:SER391 4.1 36.3 1.0
N A:ALA302 4.2 33.5 1.0
CA A:HIS303 4.3 36.7 1.0
CA A:ALA302 4.3 34.9 1.0
OE2 A:GLU346 4.4 33.7 1.0
CA A:ASN301 4.4 30.8 1.0
CG2 A:THR393 4.5 40.3 1.0
O A:HOH905 4.8 29.1 1.0
N A:THR393 4.8 40.0 1.0
ND2 A:ASN301 4.8 29.1 1.0
NZ A:LYS332 4.8 30.0 1.0
CB A:ASN392 4.8 37.7 1.0
O A:SER391 4.9 35.6 1.0

Magnesium binding site 2 out of 4 in 1oxh

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Magnesium binding site 2 out of 4 in the The Crystal Structure of Beta-Ketoacyl-[Acyl Carrier Protein] Synthase II From Streptococcus Pneumoniae, Triclinic Form


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 Beta-Ketoacyl-[Acyl Carrier Protein] Synthase II From Streptococcus Pneumoniae, Triclinic Form within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg902

b:29.9
occ:1.00
 OE1 B:GLU346 2.5 36.2 1.0
OG B:SER391 2.5 37.0 1.0
O B:ASN392 2.7 39.4 1.0
OD1 B:ASN301 2.7 39.8 1.0
O B:ASN301 2.8 38.1 1.0
O B:ALA302 2.9 40.3 1.0
N B:ASN392 3.4 37.7 1.0
C B:ALA302 3.5 40.7 1.0
CD B:GLU346 3.5 36.5 1.0
C B:ASN301 3.5 38.7 1.0
C B:ASN392 3.6 38.9 1.0
CB B:GLU346 3.7 36.2 1.0
CG B:ASN301 3.7 37.6 1.0
CB B:SER391 3.8 36.0 1.0
C B:SER391 3.9 36.4 1.0
CG B:GLU346 3.9 35.6 1.0
O B:HOH936 4.0 37.0 1.0
CA B:SER391 4.0 36.5 1.0
CA B:ASN392 4.0 38.3 1.0
N B:HIS303 4.1 40.4 1.0
N B:ALA302 4.1 39.6 1.0
CB B:ASN301 4.1 37.9 1.0
CA B:ALA302 4.3 40.9 1.0
CA B:HIS303 4.4 41.1 1.0
CA B:ASN301 4.4 37.8 1.0
OE2 B:GLU346 4.6 34.2 1.0
CG2 B:THR393 4.6 41.0 1.0
O B:HOH915 4.8 29.0 1.0
CB B:ASN392 4.8 37.9 1.0
N B:THR393 4.8 40.2 1.0
O B:SER391 4.8 36.5 1.0
ND2 B:ASN301 4.9 41.5 1.0
NZ B:LYS332 5.0 30.3 1.0

Magnesium binding site 3 out of 4 in 1oxh

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Magnesium binding site 3 out of 4 in the The Crystal Structure of Beta-Ketoacyl-[Acyl Carrier Protein] Synthase II From Streptococcus Pneumoniae, Triclinic Form


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 Beta-Ketoacyl-[Acyl Carrier Protein] Synthase II From Streptococcus Pneumoniae, Triclinic Form within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg903

b:25.1
occ:1.00
 OE1 C:GLU346 2.5 35.1 1.0
OD1 C:ASN301 2.6 38.5 1.0
O C:ASN301 2.6 36.0 1.0
O C:ASN392 2.6 39.6 1.0
OG C:SER391 2.8 36.2 1.0
O C:ALA302 3.0 39.6 1.0
N C:ASN392 3.4 38.1 1.0
C C:ALA302 3.5 39.1 1.0
CD C:GLU346 3.5 36.1 1.0
C C:ASN301 3.5 36.9 1.0
C C:ASN392 3.6 39.0 1.0
CG C:ASN301 3.7 37.0 1.0
CB C:GLU346 3.8 35.2 1.0
N C:HIS303 3.9 39.4 1.0
CB C:SER391 4.0 36.3 1.0
C C:SER391 4.0 36.5 1.0
CG C:GLU346 4.0 35.1 1.0
O C:HOH926 4.0 35.9 1.0
CA C:ASN392 4.1 38.2 1.0
CA C:SER391 4.1 36.2 1.0
CB C:ASN301 4.1 36.0 1.0
CA C:HIS303 4.2 40.0 1.0
N C:ALA302 4.3 37.9 1.0
CA C:ALA302 4.3 39.1 1.0
CA C:ASN301 4.4 35.3 1.0
CG2 C:THR393 4.5 40.6 1.0
OE2 C:GLU346 4.5 33.6 1.0
O C:HOH907 4.6 29.9 1.0
N C:THR393 4.7 40.0 1.0
CB C:ASN392 4.8 37.8 1.0
NZ C:LYS332 4.8 30.0 1.0
ND2 C:ASN301 4.8 37.6 1.0
O C:SER391 4.9 35.9 1.0

Magnesium binding site 4 out of 4 in 1oxh

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Magnesium binding site 4 out of 4 in the The Crystal Structure of Beta-Ketoacyl-[Acyl Carrier Protein] Synthase II From Streptococcus Pneumoniae, Triclinic Form


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 Beta-Ketoacyl-[Acyl Carrier Protein] Synthase II From Streptococcus Pneumoniae, Triclinic Form within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg904

b:21.4
occ:1.00
 OE1 D:GLU346 2.5 35.8 1.0
OD1 D:ASN301 2.6 37.5 1.0
O D:ASN392 2.6 38.7 1.0
OG D:SER391 2.6 36.7 1.0
O D:ALA302 2.7 38.5 1.0
O D:ASN301 2.8 33.8 1.0
N D:ASN392 3.3 37.3 1.0
CD D:GLU346 3.4 36.3 1.0
C D:ALA302 3.5 37.8 1.0
C D:ASN301 3.5 34.5 1.0
C D:ASN392 3.5 38.9 1.0
CG D:ASN301 3.6 34.4 1.0
CB D:GLU346 3.7 35.7 1.0
CB D:SER391 3.8 36.2 1.0
CG D:GLU346 3.9 35.6 1.0
C D:SER391 3.9 36.3 1.0
CA D:ASN392 4.0 38.2 1.0
CB D:ASN301 4.0 34.3 1.0
CA D:SER391 4.0 36.4 1.0
N D:HIS303 4.0 38.2 1.0
O D:HOH938 4.0 36.4 1.0
N D:ALA302 4.1 35.0 1.0
CA D:ALA302 4.3 37.1 1.0
CA D:HIS303 4.3 38.8 1.0
CA D:ASN301 4.4 35.0 1.0
OE2 D:GLU346 4.5 34.4 1.0
CG2 D:THR393 4.5 40.7 1.0
N D:THR393 4.7 40.0 1.0
O D:HOH918 4.7 28.5 1.0
CB D:ASN392 4.8 38.0 1.0
O D:SER391 4.8 36.2 1.0
ND2 D:ASN301 4.8 35.4 1.0
NZ D:LYS332 4.9 30.2 1.0

Reference:

A.C.Price, C.O.Rock, S.W.White. The 1.3-Angstrom-Resolution Crystal Structure of Beta-Ketoacyl-Acyl Carrier Protein Synthase II From Streptococcus Pneumoniae. J.Bacteriol. V. 185 4136 2003.
ISSN: ISSN 0021-9193
PubMed: 12837788
DOI: 10.1128/JB.185.14.4136-4143.2003
Page generated: Tue Aug 13 10:44:19 2024

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