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Manganese in PDB 6oqz: Crystal Structure of Glucose Isomerase From Non-Merohedrally Twinned Crystals

Enzymatic activity of Crystal Structure of Glucose Isomerase From Non-Merohedrally Twinned Crystals

All present enzymatic activity of Crystal Structure of Glucose Isomerase From Non-Merohedrally Twinned Crystals:
5.3.1.5;

Protein crystallography data

The structure of Crystal Structure of Glucose Isomerase From Non-Merohedrally Twinned Crystals, PDB code: 6oqz was solved by M.Sevvana, M.Ruf, I.Uson, G.M.Sheldrick, R.Herbst-Irmer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 70.88 / 1.60
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 92.931, 97.935, 102.706, 90.00, 90.00, 90.00
R / Rfree (%) n/a / n/a

Other elements in 6oqz:

The structure of Crystal Structure of Glucose Isomerase From Non-Merohedrally Twinned Crystals also contains other interesting chemical elements:

Magnesium (Mg) 1 atom

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of Glucose Isomerase From Non-Merohedrally Twinned Crystals (pdb code 6oqz). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Crystal Structure of Glucose Isomerase From Non-Merohedrally Twinned Crystals, PDB code: 6oqz:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 6oqz

Go back to Manganese Binding Sites List in 6oqz
Manganese binding site 1 out of 2 in the Crystal Structure of Glucose Isomerase From Non-Merohedrally Twinned Crystals


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of Glucose Isomerase From Non-Merohedrally Twinned Crystals within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn401

b:12.6
occ:1.00
OD2 A:ASP255 1.8 12.5 1.0
OE2 A:GLU217 2.0 12.4 1.0
O A:HOH636 2.0 13.3 1.0
OD1 A:ASP257 2.1 12.4 1.0
NE2 A:HIS220 2.2 12.1 1.0
CG A:ASP255 2.4 11.1 1.0
OD1 A:ASP255 2.5 11.6 1.0
CD2 A:HIS220 3.0 6.7 1.0
CD A:GLU217 3.0 9.2 1.0
CG A:ASP257 3.1 13.6 1.0
CE1 A:HIS220 3.2 12.5 1.0
OE1 A:GLU217 3.2 12.5 1.0
OD2 A:ASP257 3.3 17.1 1.0
O A:HOH674 3.6 17.2 1.0
CB A:ASP255 3.9 9.8 1.0
O A:HOH510 4.0 9.2 1.0
ND2 A:ASN247 4.0 9.6 1.0
CG A:HIS220 4.1 5.1 1.0
ND1 A:HIS220 4.2 10.0 1.0
CG A:GLU217 4.3 6.3 1.0
CB A:ASP257 4.5 11.3 1.0
CE A:LYS183 4.6 11.1 1.0
OD2 A:ASP287 4.8 15.8 1.0
CA A:ASP257 4.9 9.6 1.0
CA A:ASP255 4.9 9.1 1.0
NZ A:LYS183 5.0 13.3 1.0
MN A:MN402 5.0 9.5 0.4
MG A:MG403 5.0 9.5 0.6
N A:ASP257 5.0 11.7 1.0

Manganese binding site 2 out of 2 in 6oqz

Go back to Manganese Binding Sites List in 6oqz
Manganese binding site 2 out of 2 in the Crystal Structure of Glucose Isomerase From Non-Merohedrally Twinned Crystals


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of Glucose Isomerase From Non-Merohedrally Twinned Crystals within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn402

b:9.5
occ:0.39
MG A:MG403 0.0 9.5 0.6
OD2 A:ASP287 1.9 15.8 1.0
OE2 A:GLU181 2.0 15.2 1.0
OE1 A:GLU217 2.0 12.5 1.0
O A:HOH504 2.3 27.1 1.0
OD2 A:ASP245 2.3 14.9 1.0
CG A:ASP287 2.9 14.7 1.0
CD A:GLU181 3.0 15.1 1.0
CD A:GLU217 3.1 9.2 1.0
CG A:ASP245 3.2 20.3 1.0
CB A:ASP287 3.2 11.5 1.0
OE1 A:GLU181 3.3 16.9 1.0
CM A:MPD404 3.4 30.7 1.0
CB A:ASP245 3.8 16.5 1.0
CG A:GLU217 3.8 6.3 1.0
O A:HOH636 3.9 13.3 1.0
CB A:GLU217 4.0 8.5 1.0
OD1 A:ASP287 4.0 13.6 1.0
OD1 A:ASP245 4.0 32.5 1.0
C3 A:MPD404 4.1 21.8 1.0
O2 A:MPD404 4.1 31.1 1.0
C2 A:MPD404 4.1 29.2 1.0
OE2 A:GLU217 4.1 12.4 1.0
CG A:GLU181 4.3 12.7 1.0
CE1 A:HIS220 4.3 12.5 1.0
C4 A:MPD404 4.7 27.4 1.0
CA A:ASP287 4.8 7.9 1.0
NE2 A:HIS220 4.9 12.1 1.0
ND1 A:HIS220 5.0 10.0 1.0
MN A:MN401 5.0 12.6 1.0
ND2 A:ASN215 5.0 11.6 1.0

Reference:

M.Sevvana, M.Ruf, I.Uson, G.M.Sheldrick, R.Herbst-Irmer. Non-Merohedral Twinning: From Minerals to Proteins. Acta Crystallogr D Struct V. 75 1040 2019BIOL.
ISSN: ISSN 2059-7983
PubMed: 31793898
DOI: 10.1107/S2059798319010179
Page generated: Sun Oct 6 05:46:47 2024

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