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Magnesium in PDB 5gr5: Crystal Structure of Branching Enzyme W610A Mutant From Cyanothece Sp. Atcc 51142

Enzymatic activity of Crystal Structure of Branching Enzyme W610A Mutant From Cyanothece Sp. Atcc 51142

All present enzymatic activity of Crystal Structure of Branching Enzyme W610A Mutant From Cyanothece Sp. Atcc 51142:
2.4.1.18;

Protein crystallography data

The structure of Crystal Structure of Branching Enzyme W610A Mutant From Cyanothece Sp. Atcc 51142, PDB code: 5gr5 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) 46.25 / 2.40
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 133.870, 133.870, 185.010, 90.00, 90.00, 90.00
R / Rfree (%) 15.1 / 18.7

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Branching Enzyme W610A Mutant From Cyanothece Sp. Atcc 51142 (pdb code 5gr5). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Crystal Structure of Branching Enzyme W610A Mutant From Cyanothece Sp. Atcc 51142, PDB code: 5gr5:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in 5gr5

Go back to Magnesium Binding Sites List in 5gr5
Magnesium binding site 1 out of 3 in the Crystal Structure of Branching Enzyme W610A 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 W610A Mutant From Cyanothece Sp. Atcc 51142 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg805

b:22.4
occ:1.00
O A:HOH1237 1.9 15.7 1.0
O A:HOH1101 1.9 22.1 1.0
OD1 A:ASP612 2.0 15.7 1.0
O A:HOH958 2.0 15.8 1.0
O A:HOH1019 2.1 13.9 1.0
CG A:ASP612 3.1 17.2 1.0
O A:HOH1060 3.6 28.7 1.0
OD2 A:ASP612 3.7 14.7 1.0
O A:ASP612 4.1 17.2 1.0
N A:ASP612 4.1 19.7 1.0
O A:LEU613 4.2 15.2 1.0
O A:HOH1033 4.2 23.8 1.0
O A:HOH1013 4.2 18.3 1.0
CB A:ASP612 4.4 18.0 1.0
C A:ASP612 4.4 17.4 1.0
CA A:ASP612 4.5 18.1 1.0
O A:HOH1299 4.6 26.5 1.0
OE2 A:GLU614 4.9 36.1 1.0

Magnesium binding site 2 out of 3 in 5gr5

Go back to Magnesium Binding Sites List in 5gr5
Magnesium binding site 2 out of 3 in the Crystal Structure of Branching Enzyme W610A 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 W610A Mutant From Cyanothece Sp. Atcc 51142 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg806

b:31.3
occ:1.00
O A:HOH1414 2.1 28.3 1.0
O A:HOH920 2.2 28.5 1.0
O A:HOH1043 2.2 31.8 1.0
O A:HOH1265 2.2 26.8 1.0
O A:HOH1041 4.0 28.7 1.0
OE1 A:GLU194 4.0 21.9 1.0
O A:TRP163 4.2 19.6 1.0
OD1 A:ASP164 4.3 22.9 1.0
CA A:ASP164 4.5 21.6 1.0
OE2 A:GLU194 4.5 20.8 1.0
O A:HOH1206 4.6 34.3 1.0
O A:HOH1274 4.6 36.9 1.0
CD A:GLU194 4.7 21.3 1.0
N A:GLY165 4.9 22.1 1.0
CG A:ASP164 4.9 23.6 1.0
CB A:ASP164 4.9 25.1 1.0

Magnesium binding site 3 out of 3 in 5gr5

Go back to Magnesium Binding Sites List in 5gr5
Magnesium binding site 3 out of 3 in the Crystal Structure of Branching Enzyme W610A 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 3 of Crystal Structure of Branching Enzyme W610A Mutant From Cyanothece Sp. Atcc 51142 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg807

b:51.4
occ:1.00
O A:HOH969 2.3 23.4 1.0
O A:HOH1394 2.8 45.4 1.0
OD1 A:ASN535 3.8 31.2 1.0
ND1 A:HIS532 4.0 18.1 1.0
O A:HOH978 4.1 32.0 1.0
ND2 A:ASN534 4.2 20.6 1.0
CE1 A:HIS532 4.5 17.5 1.0
OD1 A:ASN534 4.6 19.4 1.0
CG A:ASN535 4.8 26.2 1.0
CG A:ASN534 4.8 20.4 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 10:25:36 2025

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