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Magnesium in PDB 5gqx: Crystal Structure of Branching Enzyme W610N Mutant From Cyanothece Sp. Atcc 51142 in Complex with Maltoheptaose

Enzymatic activity of Crystal Structure of Branching Enzyme W610N Mutant From Cyanothece Sp. Atcc 51142 in Complex with Maltoheptaose

All present enzymatic activity of Crystal Structure of Branching Enzyme W610N Mutant From Cyanothece Sp. Atcc 51142 in Complex with Maltoheptaose:
2.4.1.18;

Protein crystallography data

The structure of Crystal Structure of Branching Enzyme W610N Mutant From Cyanothece Sp. Atcc 51142 in Complex with Maltoheptaose, PDB code: 5gqx 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 / 2.30
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 134.025, 134.025, 185.060, 90.00, 90.00, 90.00
R / Rfree (%) 14.9 / 18.4

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Branching Enzyme W610N Mutant From Cyanothece Sp. Atcc 51142 in Complex with Maltoheptaose (pdb code 5gqx). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of Branching Enzyme W610N Mutant From Cyanothece Sp. Atcc 51142 in Complex with Maltoheptaose, PDB code: 5gqx:

Magnesium binding site 1 out of 1 in 5gqx

Go back to Magnesium Binding Sites List in 5gqx
Magnesium binding site 1 out of 1 in the Crystal Structure of Branching Enzyme W610N 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 W610N Mutant From Cyanothece Sp. Atcc 51142 in Complex with Maltoheptaose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg842

b:23.6
occ:1.00
 O A:HOH1199 1.9 23.4 1.0
O A:HOH1138 2.0 22.4 1.0
O A:HOH1090 2.0 22.9 1.0
OD1 A:ASP612 2.0 15.4 1.0
O A:HOH1039 2.1 16.1 1.0
CG A:ASP612 3.2 18.0 1.0
OD2 A:ASP612 3.8 15.9 1.0
O A:HOH1202 3.8 33.7 1.0
O A:ASP612 4.1 17.1 1.0
N A:ASP612 4.1 20.1 1.0
O A:LEU613 4.1 17.7 1.0
O A:HOH1029 4.2 21.5 1.0
O A:HOH1134 4.3 23.2 1.0
C A:ASP612 4.3 17.7 1.0
CB A:ASP612 4.4 19.1 1.0
CA A:ASP612 4.5 18.5 1.0
O A:HOH1229 4.5 37.9 1.0
OE2 A:GLU614 4.9 41.6 1.0

Reference:

M.Hayashi, R.Suzuki, C.Colleoni, S.G.Ball, N.Fujita, E.Suzuki. Bound Substrate in the Structure of Cyanobacterial Branching Enzyme Supports A New Mechanistic Model J. Biol. Chem. V. 292 5465 2017.
ISSN: ESSN 1083-351X
PubMed: 28193843
DOI: 10.1074/JBC.M116.755629
Page generated: Sun Sep 29 15:22:11 2024

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