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Magnesium in PDB 5gr3: Crystal Structure of Branching Enzyme L541A/W655A Mutant From Cyanothece Sp. Atcc 51142

Enzymatic activity of Crystal Structure of Branching Enzyme L541A/W655A Mutant From Cyanothece Sp. Atcc 51142

All present enzymatic activity of Crystal Structure of Branching Enzyme L541A/W655A Mutant From Cyanothece Sp. Atcc 51142:
2.4.1.18;

Protein crystallography data

The structure of Crystal Structure of Branching Enzyme L541A/W655A Mutant From Cyanothece Sp. Atcc 51142, PDB code: 5gr3 was solved by R.Suzuki, E.Suzuki, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.38 / 2.60
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 133.616, 133.616, 185.519, 90.00, 90.00, 90.00
R / Rfree (%) 15.4 / 18.9

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Branching Enzyme L541A/W655A Mutant From Cyanothece Sp. Atcc 51142 (pdb code 5gr3). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of Branching Enzyme L541A/W655A Mutant From Cyanothece Sp. Atcc 51142, PDB code: 5gr3:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 5gr3

Go back to Magnesium Binding Sites List in 5gr3
Magnesium binding site 1 out of 2 in the Crystal Structure of Branching Enzyme L541A/W655A Mutant From Cyanothece Sp. Atcc 51142


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 Branching Enzyme L541A/W655A Mutant From Cyanothece Sp. Atcc 51142 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg802

b:27.2
occ:1.00
OD1 A:ASP612 1.8 21.7 1.0
O A:HOH1082 1.9 16.4 1.0
O A:HOH919 2.0 21.8 1.0
O A:HOH1075 2.0 26.4 1.0
O A:HOH1018 2.1 16.1 1.0
CG A:ASP612 3.0 20.4 1.0
OD2 A:ASP612 3.5 19.6 1.0
O A:HOH962 3.6 36.0 1.0
O A:ASP612 3.9 17.7 1.0
O A:LEU613 4.0 17.8 1.0
N A:ASP612 4.1 20.7 1.0
O A:HOH1063 4.1 20.9 1.0
O A:HOH1029 4.2 30.5 1.0
CB A:ASP612 4.2 20.7 1.0
C A:ASP612 4.3 19.3 1.0
CA A:ASP612 4.4 19.9 1.0
O A:HOH1364 4.5 28.0 1.0
O A:HOH1185 4.8 25.2 1.0
C A:LEU613 4.9 19.9 1.0
OE2 A:GLU614 5.0 50.6 1.0

Magnesium binding site 2 out of 2 in 5gr3

Go back to Magnesium Binding Sites List in 5gr3
Magnesium binding site 2 out of 2 in the Crystal Structure of Branching Enzyme L541A/W655A Mutant From Cyanothece Sp. Atcc 51142


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 Branching Enzyme L541A/W655A Mutant From Cyanothece Sp. Atcc 51142 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg803

b:29.9
occ:1.00
O A:HOH1272 2.1 32.7 1.0
O A:HOH1210 2.2 23.6 1.0
O A:HOH1163 2.2 28.1 1.0
O A:HOH925 2.4 24.4 1.0
O A:HOH1265 3.9 45.3 1.0
O A:TRP163 4.0 20.0 1.0
OE1 A:GLU194 4.2 27.1 1.0
O A:HOH1056 4.2 33.5 1.0
CA A:ASP164 4.2 27.6 1.0
OD1 A:ASP164 4.3 24.5 1.0
CB A:ASP164 4.7 29.4 1.0
CG A:ASP164 4.8 29.5 1.0
N A:GLY165 4.9 26.1 1.0
OE2 A:GLU194 4.9 33.1 1.0
C A:TRP163 4.9 24.7 1.0
CD A:GLU194 4.9 29.5 1.0

Reference:

M.Hayashi, R.Suzuki, C.Colleoni, S.G.Ball, N.Fujita, E.Suzuki. Structural Basis For Substrate Binding and Catalysis of Branching Enzyme From Cyanothece Sp. Atcc 51142 To Be Published.
Page generated: Tue Aug 12 10:25:15 2025

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