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Magnesium in PDB 1rmt: Crystal Structure of Apha Class B Acid Phosphatase/Phosphotransferase Complexed with Adenosine.

Enzymatic activity of Crystal Structure of Apha Class B Acid Phosphatase/Phosphotransferase Complexed with Adenosine.

All present enzymatic activity of Crystal Structure of Apha Class B Acid Phosphatase/Phosphotransferase Complexed with Adenosine.:
3.1.3.2;

Protein crystallography data

The structure of Crystal Structure of Apha Class B Acid Phosphatase/Phosphotransferase Complexed with Adenosine., PDB code: 1rmt was solved by V.Calderone, C.Forleo, M.Benvenuti, G.M.Rossolini, M.C.Thaller, S.Mangani, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 74.54 / 1.40
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 84.740, 66.704, 88.556, 90.00, 117.13, 90.00
R / Rfree (%) 16.7 / 19.9

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Apha Class B Acid Phosphatase/Phosphotransferase Complexed with Adenosine. (pdb code 1rmt). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Crystal Structure of Apha Class B Acid Phosphatase/Phosphotransferase Complexed with Adenosine., PDB code: 1rmt:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 1rmt

Go back to Magnesium Binding Sites List in 1rmt
Magnesium binding site 1 out of 4 in the Crystal Structure of Apha Class B Acid Phosphatase/Phosphotransferase Complexed with Adenosine.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Apha Class B Acid Phosphatase/Phosphotransferase Complexed with Adenosine. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1413

b:9.6
occ:1.00
 OD2 A:ASP44 2.0 6.0 1.0
O A:ASP46 2.1 5.3 1.0
O A:HOH1775 2.1 7.6 1.0
OD1 A:ASP167 2.1 6.9 1.0
O A:HOH1797 2.1 6.6 1.0
O A:HOH1812 2.1 7.3 1.0
CG A:ASP44 3.0 6.7 1.0
CG A:ASP167 3.1 5.6 1.0
C A:ASP46 3.2 4.8 1.0
OD1 A:ASP44 3.3 7.5 1.0
OD2 A:ASP167 3.4 5.8 1.0
CA A:ASP46 3.9 6.2 1.0
N A:ASP46 3.9 7.0 1.0
OG1 A:THR48 3.9 6.4 1.0
OG A:SER168 4.0 8.0 1.0
OD2 A:ASP171 4.1 8.3 1.0
O A:HOH1503 4.1 7.9 1.0
CB A:ASP46 4.2 6.0 1.0
O A:HOH1813 4.2 19.7 1.0
N A:ASP47 4.3 5.3 1.0
CB A:ASP44 4.3 7.1 1.0
O A:HOH1530 4.4 14.4 1.0
CB A:ASP167 4.4 5.7 1.0
CB A:ASP47 4.5 5.7 1.0
N A:ASP167 4.6 6.0 1.0
N A:THR48 4.6 5.5 1.0
CA A:ASP47 4.7 5.4 1.0
C A:ASP47 4.7 5.5 1.0
C A:ILE45 4.7 7.0 1.0
N A:SER168 4.8 7.2 1.0
O A:HOH1510 4.8 9.8 1.0
O A:HOH1505 4.9 10.8 1.0
CB A:THR48 4.9 7.2 1.0
O A:HOH1641 4.9 22.7 1.0
CA A:ASP167 5.0 5.1 1.0
CB A:SER168 5.0 8.5 1.0

Magnesium binding site 2 out of 4 in 1rmt

Go back to Magnesium Binding Sites List in 1rmt
Magnesium binding site 2 out of 4 in the Crystal Structure of Apha Class B Acid Phosphatase/Phosphotransferase Complexed with Adenosine.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Apha Class B Acid Phosphatase/Phosphotransferase Complexed with Adenosine. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg1414

b:9.5
occ:1.00
 O B:HOH1831 2.0 9.3 1.0
O B:HOH1800 2.0 8.2 1.0
O B:ASP46 2.0 4.7 1.0
OD2 B:ASP44 2.1 6.7 1.0
OD1 B:ASP167 2.1 6.4 1.0
O B:HOH1818 2.1 6.3 1.0
CG B:ASP44 3.0 6.3 1.0
CG B:ASP167 3.1 4.5 1.0
C B:ASP46 3.2 5.7 1.0
OD1 B:ASP44 3.3 8.4 1.0
OD2 B:ASP167 3.4 6.2 1.0
CA B:ASP46 3.9 6.6 1.0
N B:ASP46 4.0 6.1 1.0
OG1 B:THR48 4.0 6.7 1.0
OG B:SER168 4.0 9.8 1.0
O B:HOH1523 4.1 9.7 1.0
O B:HOH1654 4.1 17.6 1.0
OD2 B:ASP171 4.1 9.0 1.0
CB B:ASP46 4.1 6.8 1.0
O B:HOH1575 4.3 13.8 1.0
N B:ASP47 4.3 6.2 1.0
CB B:ASP44 4.4 6.9 1.0
CB B:ASP167 4.5 5.3 1.0
CB B:ASP47 4.6 5.2 1.0
N B:THR48 4.6 4.9 1.0
N B:ASP167 4.6 5.7 1.0
CA B:ASP47 4.7 6.2 1.0
C B:ASP47 4.7 5.4 1.0
C B:ILE45 4.8 5.9 1.0
N B:SER168 4.8 6.7 1.0
O B:HOH1512 4.8 8.7 1.0
O B:HOH1530 4.9 12.1 1.0
CB B:SER168 4.9 8.3 1.0
CB B:THR48 4.9 5.9 1.0
CA B:ASP167 5.0 5.6 1.0

Magnesium binding site 3 out of 4 in 1rmt

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Magnesium binding site 3 out of 4 in the Crystal Structure of Apha Class B Acid Phosphatase/Phosphotransferase Complexed with Adenosine.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of Apha Class B Acid Phosphatase/Phosphotransferase Complexed with Adenosine. within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg1415

b:12.4
occ:1.00
 OD2 C:ASP44 2.0 9.0 1.0
OD1 C:ASP167 2.1 8.1 1.0
O C:ASP46 2.1 7.3 1.0
O C:HOH1787 2.1 11.4 1.0
O C:HOH1771 2.1 9.2 1.0
O C:HOH1750 2.1 10.7 1.0
CG C:ASP44 3.0 9.6 1.0
CG C:ASP167 3.1 7.1 1.0
C C:ASP46 3.3 7.1 1.0
OD2 C:ASP167 3.4 8.6 1.0
OD1 C:ASP44 3.4 10.6 1.0
OG C:SER168 4.0 10.6 1.0
OG1 C:THR48 4.0 8.3 1.0
O C:HOH1671 4.0 33.5 1.0
CA C:ASP46 4.0 8.0 1.0
OD2 C:ASP171 4.0 11.6 1.0
N C:ASP46 4.0 8.7 1.0
O2' C:ADN1503 4.1 36.3 1.0
O C:HOH1526 4.1 16.7 1.0
CB C:ASP46 4.2 8.6 1.0
O C:HOH1531 4.2 11.5 1.0
CB C:ASP44 4.3 8.5 1.0
O C:HOH1504 4.4 10.9 1.0
N C:ASP47 4.4 7.0 1.0
CB C:ASP167 4.4 8.1 1.0
N C:ASP167 4.6 7.8 1.0
CB C:ASP47 4.6 7.6 1.0
N C:THR48 4.6 6.8 1.0
CA C:ASP47 4.7 7.4 1.0
C C:ASP47 4.8 6.5 1.0
C C:ILE45 4.8 8.8 1.0
C2' C:ADN1503 4.8 35.4 1.0
CB C:SER168 4.8 8.9 1.0
N C:SER168 4.8 7.8 1.0
CB C:THR48 4.9 7.8 1.0
CA C:ASP167 5.0 7.0 1.0

Magnesium binding site 4 out of 4 in 1rmt

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Magnesium binding site 4 out of 4 in the Crystal Structure of Apha Class B Acid Phosphatase/Phosphotransferase Complexed with Adenosine.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Crystal Structure of Apha Class B Acid Phosphatase/Phosphotransferase Complexed with Adenosine. within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg1416

b:10.2
occ:1.00
 OD2 D:ASP44 2.0 6.5 1.0
O D:HOH1778 2.1 6.8 1.0
O D:ASP46 2.1 5.4 1.0
OD1 D:ASP167 2.1 6.8 1.0
O D:HOH1797 2.1 9.0 1.0
O D:HOH1811 2.1 10.0 1.0
CG D:ASP44 3.0 7.1 1.0
CG D:ASP167 3.1 5.8 1.0
C D:ASP46 3.2 6.2 1.0
OD1 D:ASP44 3.4 7.2 1.0
OD2 D:ASP167 3.4 6.9 1.0
OG1 D:THR48 3.9 6.1 1.0
CA D:ASP46 4.0 7.2 1.0
OG D:SER168 4.0 9.8 1.0
OD2 D:ASP171 4.0 8.2 1.0
O2' D:ADN1504 4.1 28.8 1.0
N D:ASP46 4.1 6.9 1.0
CB D:ASP46 4.1 7.3 1.0
O D:HOH1523 4.2 12.1 1.0
CB D:ASP44 4.3 6.4 1.0
O D:HOH1510 4.3 10.2 1.0
N D:ASP47 4.3 6.5 1.0
O D:HOH1537 4.4 15.0 1.0
CB D:ASP167 4.4 7.0 1.0
CB D:ASP47 4.6 6.1 1.0
N D:ASP167 4.6 5.8 1.0
N D:THR48 4.7 5.8 1.0
CA D:ASP47 4.7 5.6 1.0
C D:ASP47 4.8 5.8 1.0
C D:ILE45 4.8 7.4 1.0
N D:SER168 4.8 7.4 1.0
CB D:SER168 4.9 9.2 1.0
CB D:THR48 4.9 6.9 1.0
C2' D:ADN1504 5.0 31.9 1.0
CA D:ASP167 5.0 6.1 1.0

Reference:

V.Calderone, C.Forleo, M.Benvenuti, G.M.Rossolini, M.C.Thaller, S.Mangani. Insights in the Catalytic Mechanism of Apha From Escherichia Coli To Be Published.
Page generated: Tue Aug 13 13:03:27 2024

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