Magnesium in PDB 5gr1: Crystal Structure of Branching Enzyme Y500A/D501A Mutant From Cyanothece Sp. Atcc 51142 in Complex with Maltoheptaose

All present enzymatic activity of Crystal Structure of Branching Enzyme Y500A/D501A Mutant From Cyanothece Sp. Atcc 51142 in Complex with Maltoheptaose:
2.4.1.18;

The structure of Crystal Structure of Branching Enzyme Y500A/D501A Mutant From Cyanothece Sp. Atcc 51142 in Complex with Maltoheptaose, PDB code: 5gr1 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)	47.38 / 2.50
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	134.001, 134.001, 181.511, 90.00, 90.00, 90.00
R / Rfree (%)	18.2 / 22.7

The binding sites of Magnesium atom in the Crystal Structure of Branching Enzyme Y500A/D501A Mutant From Cyanothece Sp. Atcc 51142 in Complex with Maltoheptaose (pdb code 5gr1). 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 Y500A/D501A Mutant From Cyanothece Sp. Atcc 51142 in Complex with Maltoheptaose, PDB code: 5gr1:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Branching Enzyme Y500A/D501A Mutant From Cyanothece Sp. Atcc 51142 in Complex with Maltoheptaose


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 Y500A/D501A Mutant From Cyanothece Sp. Atcc 51142 in Complex with Maltoheptaose within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg826 b:51.8 occ:1.00 O A:HOH924 2.0 45.6 1.0 O A:HOH1124 2.1 41.6 1.0 O A:HOH1190 2.3 38.4 1.0 OD1 A:ASP434 3.5 44.9 1.0 OE1 A:GLU487 3.6 49.8 1.0 CB A:ALA435 4.2 30.5 1.0 O A:HOH1216 4.2 49.1 1.0 O A:HOH1014 4.2 39.6 1.0 OD2 A:ASP555 4.3 40.5 1.0 CD A:GLU487 4.4 39.9 1.0 O A:HOH965 4.4 37.2 1.0 O A:HOH1052 4.5 19.4 1.0 OE2 A:GLU487 4.6 33.1 1.0 CA A:ALA435 4.6 32.6 1.0 CG A:ASP434 4.7 46.5 1.0 N A:ALA435 4.8 32.7 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Branching Enzyme Y500A/D501A Mutant From Cyanothece Sp. Atcc 51142 in Complex with Maltoheptaose


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 Y500A/D501A Mutant From Cyanothece Sp. Atcc 51142 in Complex with Maltoheptaose within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg827 b:40.0 occ:1.00 O A:HOH1072 1.8 38.9 1.0 O A:HOH1008 1.9 33.8 1.0 O A:HOH931 2.0 18.0 1.0 OD1 A:ASP612 2.0 29.3 1.0 O A:HOH939 2.2 23.6 1.0 CG A:ASP612 3.2 33.1 1.0 O A:HOH997 3.6 36.9 1.0 OD2 A:ASP612 3.8 27.4 1.0 O A:LEU613 4.1 26.6 1.0 O A:HOH1050 4.2 28.0 1.0 N A:ASP612 4.3 32.1 1.0 O A:ASP612 4.3 31.2 1.0 CB A:ASP612 4.4 33.0 1.0 O A:HOH1005 4.5 44.8 1.0 C A:ASP612 4.5 29.7 1.0 CA A:ASP612 4.6 29.5 1.0

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.