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

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

The structure of Crystal Structure of Branching Enzyme From Cyanothece Sp. Atcc 51142, PDB code: 5gqu 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)	47.29 / 1.85
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	133.750, 133.750, 185.902, 90.00, 90.00, 90.00
R / Rfree (%)	14.7 / 17

The binding sites of Magnesium atom in the Crystal Structure of Branching Enzyme From Cyanothece Sp. Atcc 51142 (pdb code 5gqu). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Crystal Structure of Branching Enzyme From Cyanothece Sp. Atcc 51142, PDB code: 5gqu:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in the Crystal Structure of Branching Enzyme 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 From Cyanothece Sp. Atcc 51142 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg808 b:40.6 occ:1.00 O A:HOH1577 2.2 40.2 1.0 O A:HOH1655 2.2 31.6 1.0 O A:HOH903 2.2 50.2 1.0 O A:HOH1430 2.2 34.0 1.0 OE1 A:GLU487 4.1 27.3 1.0 O A:HOH1154 4.2 31.1 1.0 OD1 A:ASP434 4.3 36.7 1.0 O A:HOH1006 4.3 23.8 1.0 OD2 A:ASP555 4.5 32.3 1.0 CD A:GLU487 4.7 23.8 1.0 O A:HOH977 4.8 30.0 1.0 OE2 A:GLU487 4.8 27.5 1.0 O A:HOH1454 4.8 17.4 1.0 CB A:ALA435 4.8 24.0 1.0

Magnesium binding site 2 out of 4 in the Crystal Structure of Branching Enzyme 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 From Cyanothece Sp. Atcc 51142 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg809 b:22.5 occ:1.00 OD1 A:ASP612 2.0 17.6 1.0 O A:HOH1512 2.1 26.4 1.0 O A:HOH1355 2.1 25.9 1.0 O A:HOH1096 2.1 21.5 1.0 O A:HOH1158 2.1 22.2 1.0 CG A:ASP612 3.1 16.8 1.0 OD2 A:ASP612 3.7 18.2 1.0 O A:HOH1198 3.8 34.5 1.0 O A:ASP612 4.0 14.9 1.0 O A:LEU613 4.0 16.4 1.0 N A:ASP612 4.2 15.5 1.0 O A:HOH1713 4.3 36.2 1.0 O A:HOH1106 4.3 29.5 1.0 O A:HOH1211 4.3 22.1 1.0 C A:ASP612 4.3 16.1 1.0 CB A:ASP612 4.3 15.0 1.0 CA A:ASP612 4.4 14.0 1.0 O A:HOH1485 4.5 27.5 1.0 C A:LEU613 4.9 17.2 1.0 OE1 A:GLU614 5.0 42.4 1.0

Magnesium binding site 3 out of 4 in the Crystal Structure of Branching Enzyme 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 From Cyanothece Sp. Atcc 51142 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg810 b:23.9 occ:1.00 O A:HOH1600 2.0 23.4 1.0 O A:HOH1476 2.1 22.7 1.0 O A:HOH1115 2.1 24.7 1.0 O A:HOH1008 2.2 22.9 1.0 O A:HOH1209 3.9 26.3 1.0 OE1 A:GLU194 4.1 22.4 1.0 O A:TRP163 4.2 20.5 1.0 OD1 A:ASP164 4.3 22.4 1.0 CA A:ASP164 4.4 18.9 1.0 OE2 A:GLU194 4.4 25.1 1.0 O A:HOH1424 4.6 37.1 1.0 O A:HOH1460 4.6 41.7 1.0 CD A:GLU194 4.7 23.4 1.0 N A:GLY165 4.8 20.7 1.0 CG A:ASP164 4.9 24.4 1.0 CB A:ASP164 4.9 22.3 1.0

Magnesium binding site 4 out of 4 in the Crystal Structure of Branching Enzyme 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 4 of Crystal Structure of Branching Enzyme From Cyanothece Sp. Atcc 51142 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg811 b:44.0 occ:1.00 O A:HOH1574 2.1 36.5 1.0 O A:HOH924 2.2 44.7 1.0 O A:HOH1012 2.2 28.2 1.0 O A:HOH1418 3.9 34.4 1.0 OD1 A:ASN535 4.1 29.7 1.0 ND2 A:ASN534 4.2 25.8 1.0 ND1 A:HIS532 4.2 23.0 1.0 O A:HOH964 4.2 33.0 1.0 OD1 A:ASN534 4.5 21.8 1.0 CE1 A:HIS532 4.7 23.6 1.0 CG A:ASN534 4.8 22.1 1.0

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