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Magnesium in PDB 1pg3: Acetyl Coa Synthetase, Acetylated on LYS609

Enzymatic activity of Acetyl Coa Synthetase, Acetylated on LYS609

All present enzymatic activity of Acetyl Coa Synthetase, Acetylated on LYS609:
6.2.1.1;

Protein crystallography data

The structure of Acetyl Coa Synthetase, Acetylated on LYS609, PDB code: 1pg3 was solved by A.M.Gulick, V.J.Starai, A.R.Horswill, K.M.Homick, J.C.Escalante-Semerena, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.22 / 2.30
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 59.981, 143.160, 71.934, 90.00, 91.57, 90.00
R / Rfree (%) 19.6 / 23.6

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Acetyl Coa Synthetase, Acetylated on LYS609 (pdb code 1pg3). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Acetyl Coa Synthetase, Acetylated on LYS609, PDB code: 1pg3:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 1pg3

Go back to Magnesium Binding Sites List in 1pg3
Magnesium binding site 1 out of 2 in the Acetyl Coa Synthetase, Acetylated on LYS609


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Acetyl Coa Synthetase, Acetylated on LYS609 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg902

b:15.2
occ:1.00
O A:VAL537 2.4 17.8 1.0
O A:HIS539 2.5 20.4 1.0
O A:ILE542 2.6 19.9 1.0
O A:HOH1097 2.6 22.6 1.0
O A:HOH1198 2.7 30.0 1.0
O A:HOH1200 2.8 33.6 1.0
C A:HIS539 3.4 21.1 1.0
C A:VAL537 3.6 18.2 1.0
C A:ILE542 3.7 20.1 1.0
C A:ALA538 4.1 19.5 1.0
N A:HIS539 4.1 19.8 1.0
N A:PRO540 4.1 22.3 1.0
CA A:PRO540 4.2 22.4 1.0
N A:ILE542 4.2 19.6 1.0
C A:PRO540 4.2 22.5 1.0
O A:ALA538 4.3 19.5 1.0
CA A:ILE542 4.4 20.4 1.0
CG1 A:VAL537 4.4 17.9 1.0
CA A:HIS539 4.4 20.2 1.0
O A:PRO540 4.4 23.1 1.0
CA A:ALA538 4.5 18.2 1.0
N A:ALA538 4.5 17.4 1.0
CA A:VAL537 4.5 17.6 1.0
ND2 A:ASN566 4.7 27.9 1.0
N A:LYS541 4.7 21.5 1.0
N A:ALA543 4.8 21.6 1.0
CB A:ILE542 4.8 19.5 1.0
CA A:ALA543 4.9 23.1 1.0

Magnesium binding site 2 out of 2 in 1pg3

Go back to Magnesium Binding Sites List in 1pg3
Magnesium binding site 2 out of 2 in the Acetyl Coa Synthetase, Acetylated on LYS609


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Acetyl Coa Synthetase, Acetylated on LYS609 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg901

b:21.9
occ:1.00
O B:HIS539 2.5 22.0 1.0
O B:VAL537 2.5 13.1 1.0
O B:HOH1137 2.6 24.9 1.0
O B:ILE542 2.6 20.0 1.0
O B:HOH1148 3.0 35.6 1.0
C B:HIS539 3.4 21.5 1.0
O B:HOH1150 3.4 44.1 1.0
C B:VAL537 3.6 15.0 1.0
C B:ILE542 3.8 20.4 1.0
CA B:PRO540 4.1 23.1 1.0
C B:ALA538 4.1 17.9 1.0
O B:PRO540 4.1 23.7 1.0
N B:PRO540 4.1 22.1 1.0
C B:PRO540 4.1 23.6 1.0
N B:HIS539 4.2 18.2 1.0
N B:ILE542 4.2 22.8 1.0
O B:ALA538 4.2 17.9 1.0
CG1 B:VAL537 4.4 12.8 1.0
CA B:HIS539 4.4 20.0 1.0
CA B:VAL537 4.5 15.1 1.0
CA B:ILE542 4.5 20.8 1.0
N B:ALA538 4.5 14.2 1.0
CA B:ALA538 4.6 16.0 1.0
ND2 B:ASN566 4.7 22.5 1.0
N B:LYS541 4.8 23.3 1.0
N B:ALA543 4.8 19.3 1.0
CB B:ILE542 4.9 20.6 1.0
O B:HOH1149 4.9 24.8 1.0

Reference:

A.M.Gulick, V.J.Starai, A.R.Horswill, K.M.Homick, J.C.Escalante-Semerena. The 1.75 A Crystal Structure of Acetyl-Coa Synthetase Bound to Adenosine-5'-Propylphosphate and Coenzyme A Biochemistry V. 42 2866 2003.
ISSN: ISSN 0006-2960
PubMed: 12627952
DOI: 10.1021/BI0271603
Page generated: Tue Aug 13 10:51:31 2024

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