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Magnesium in PDB 5gqv: Crystal Structure of Branching Enzyme From Cyanothece Sp. Atcc 51142 in Complex with Maltohexaose

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

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

Protein crystallography data

The structure of Crystal Structure of Branching Enzyme From Cyanothece Sp. Atcc 51142 in Complex with Maltohexaose, PDB code: 5gqv 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) 47.42 / 3.00
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 134.126, 134.126, 184.325, 90.00, 90.00, 90.00
R / Rfree (%) 16.3 / 22.4

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Branching Enzyme From Cyanothece Sp. Atcc 51142 in Complex with Maltohexaose (pdb code 5gqv). 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 From Cyanothece Sp. Atcc 51142 in Complex with Maltohexaose, PDB code: 5gqv:

Magnesium binding site 1 out of 1 in 5gqv

Go back to Magnesium Binding Sites List in 5gqv
Magnesium binding site 1 out of 1 in the Crystal Structure of Branching Enzyme From Cyanothece Sp. Atcc 51142 in Complex with Maltohexaose


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 From Cyanothece Sp. Atcc 51142 in Complex with Maltohexaose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg840

b:14.4
occ:1.00
 OD1 A:ASP612 1.9 33.1 1.0
O A:HOH996 2.3 13.3 1.0
O A:HOH946 2.4 22.0 1.0
O A:HOH958 2.5 13.0 1.0
O A:HOH940 2.6 13.4 1.0
CG A:ASP612 2.9 33.9 1.0
OD2 A:ASP612 3.3 36.1 1.0
O A:HOH936 3.7 19.8 1.0
N A:ASP612 4.2 33.3 1.0
CB A:ASP612 4.2 34.1 1.0
O A:ASP612 4.5 29.9 1.0
CA A:ASP612 4.6 33.2 1.0
O A:HOH1032 4.6 30.4 1.0
C A:ASP612 4.6 30.1 1.0
O A:LEU613 4.6 32.8 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 15:21:44 2024

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