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Magnesium in PDB 1oad: Glucose Isomerase From Streptomyces Rubiginosus in P21212 Crystal Form

Enzymatic activity of Glucose Isomerase From Streptomyces Rubiginosus in P21212 Crystal Form

All present enzymatic activity of Glucose Isomerase From Streptomyces Rubiginosus in P21212 Crystal Form:
5.3.1.5;

Protein crystallography data

The structure of Glucose Isomerase From Streptomyces Rubiginosus in P21212 Crystal Form, PDB code: 1oad was solved by U.A.Ramagopal, M.Dauter, Z.Dauter, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.0 / 1.5
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 98.450, 129.590, 78.330, 90.00, 90.00, 90.00
R / Rfree (%) 16.3 / 18.6

Other elements in 1oad:

The structure of Glucose Isomerase From Streptomyces Rubiginosus in P21212 Crystal Form also contains other interesting chemical elements:

Manganese (Mn) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Glucose Isomerase From Streptomyces Rubiginosus in P21212 Crystal Form (pdb code 1oad). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Glucose Isomerase From Streptomyces Rubiginosus in P21212 Crystal Form, PDB code: 1oad:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 1oad

Go back to Magnesium Binding Sites List in 1oad
Magnesium binding site 1 out of 2 in the Glucose Isomerase From Streptomyces Rubiginosus in P21212 Crystal Form


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Glucose Isomerase From Streptomyces Rubiginosus in P21212 Crystal Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg392

b:11.5
occ:0.99
OD2 A:ASP245 1.9 30.0 1.0
OE2 A:GLU181 2.0 14.8 1.0
O A:HOH2321 2.0 27.5 1.0
OD2 A:ASP287 2.0 14.7 1.0
OE1 A:GLU217 2.0 13.4 1.0
O6 A:MQD395 2.6 28.0 1.0
CD A:GLU181 3.0 18.9 1.0
CG A:ASP287 3.1 14.2 1.0
CG A:ASP245 3.1 22.2 1.0
CD A:GLU217 3.1 11.6 1.0
OE1 A:GLU181 3.3 17.8 1.0
CB A:ASP287 3.4 12.8 1.0
OD1 A:ASP245 3.7 15.9 1.0
CM A:MQD395 3.9 26.2 1.0
O A:HOH2464 3.9 17.3 1.0
CG A:GLU217 4.0 10.6 1.0
O2 A:MQD395 4.0 26.1 1.0
CB A:GLU217 4.1 9.7 1.0
CB A:ASP245 4.1 21.7 1.0
C3 A:MQD395 4.1 22.9 1.0
OD1 A:ASP287 4.1 13.2 1.0
OE2 A:GLU217 4.2 14.2 1.0
CE1 A:HIS220 4.2 11.0 1.0
C2 A:MQD395 4.3 27.5 1.0
CG A:GLU181 4.3 16.0 1.0
C4 A:MQD395 4.6 20.7 1.0
MN A:MN390 4.8 14.8 1.0
NE2 A:HIS220 4.8 11.6 1.0
ND1 A:HIS220 4.9 9.8 1.0
C5 A:MQD395 4.9 25.9 1.0
CA A:ASP287 4.9 9.1 1.0
ND2 A:ASN215 5.0 13.5 1.0

Magnesium binding site 2 out of 2 in 1oad

Go back to Magnesium Binding Sites List in 1oad
Magnesium binding site 2 out of 2 in the Glucose Isomerase From Streptomyces Rubiginosus in P21212 Crystal Form


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Glucose Isomerase From Streptomyces Rubiginosus in P21212 Crystal Form within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg392

b:12.6
occ:0.99
O B:HOH2293 2.0 27.4 1.0
OD2 B:ASP245 2.0 29.6 1.0
OE2 B:GLU181 2.0 17.1 1.0
OE1 B:GLU217 2.0 15.2 1.0
OD2 B:ASP287 2.0 15.8 1.0
O6 B:MQD395 2.7 29.8 1.0
CG B:ASP287 3.0 13.4 1.0
CD B:GLU181 3.0 15.3 1.0
CG B:ASP245 3.1 22.1 1.0
CD B:GLU217 3.2 16.1 1.0
OE1 B:GLU181 3.3 16.3 1.0
CB B:ASP287 3.4 12.2 1.0
OD1 B:ASP245 3.7 16.9 1.0
O B:HOH2432 3.9 19.5 1.0
CM B:MQD395 3.9 25.6 1.0
CG B:GLU217 3.9 12.8 1.0
O2 B:MQD395 4.0 24.9 1.0
CB B:GLU217 4.0 9.6 1.0
C3 B:MQD395 4.1 22.9 1.0
OD1 B:ASP287 4.2 13.5 1.0
CB B:ASP245 4.2 23.4 1.0
OE2 B:GLU217 4.2 13.1 1.0
CE1 B:HIS220 4.2 11.8 1.0
CG B:GLU181 4.3 11.8 1.0
C2 B:MQD395 4.3 25.7 1.0
C4 B:MQD395 4.6 24.1 1.0
MN B:MN390 4.8 14.8 1.0
NE2 B:HIS220 4.8 12.0 1.0
ND1 B:HIS220 4.9 11.7 1.0
CA B:ASP287 4.9 12.8 1.0
C5 B:MQD395 4.9 24.2 1.0
ND2 B:ASN215 5.0 15.1 1.0

Reference:

U.A.Ramagopal, M.Dauter, Z.Dauter. Sad Manganese in Two Crystal Forms of Glucose Isomerase Acta Crystallogr.,Sect.D V. 59 868 2003.
ISSN: ISSN 0907-4449
PubMed: 12777803
DOI: 10.1107/S0907444903005663
Page generated: Tue Aug 13 10:35:10 2024

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