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Magnesium in PDB 8awd: Xylose Isomerase in 95% Relative Humidity Environment

Enzymatic activity of Xylose Isomerase in 95% Relative Humidity Environment

All present enzymatic activity of Xylose Isomerase in 95% Relative Humidity Environment:
5.3.1.5;

Protein crystallography data

The structure of Xylose Isomerase in 95% Relative Humidity Environment, PDB code: 8awd was solved by P.Mehrabi, S.Sung, D.Von Stetten, A.Prester, C.E.Hatton, S.Kleine-Doepke, A.Berkes, G.Gore, J.P.Leimkohl, H.Schikora, M.Kollewe, H.Rohde, M.Wilmanns, F.Tellkamp, E.C.Schulz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.55 / 1.85
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 93.48, 99.11, 102.46, 90, 90, 90
R / Rfree (%) 16 / 19.2

Other elements in 8awd:

The structure of Xylose Isomerase in 95% Relative Humidity Environment also contains other interesting chemical elements:

Manganese (Mn) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Xylose Isomerase in 95% Relative Humidity Environment (pdb code 8awd). 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 Xylose Isomerase in 95% Relative Humidity Environment, PDB code: 8awd:

Magnesium binding site 1 out of 1 in 8awd

Go back to Magnesium Binding Sites List in 8awd
Magnesium binding site 1 out of 1 in the Xylose Isomerase in 95% Relative Humidity Environment


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Xylose Isomerase in 95% Relative Humidity Environment within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg401

b:25.4
occ:0.40
OD2 A:ASP287 1.8 26.8 1.0
OE2 A:GLU181 2.0 26.2 1.0
OE1 A:GLU217 2.3 23.0 1.0
OD2 A:ASP245 2.3 21.3 1.0
O2 A:GOL402 2.5 32.6 0.7
CD A:GLU181 2.8 25.0 1.0
CG A:ASP287 2.9 26.7 1.0
OE1 A:GLU181 3.2 28.7 1.0
CB A:ASP287 3.4 24.1 1.0
CG A:ASP245 3.5 25.9 1.0
CD A:GLU217 3.5 24.7 1.0
O A:HOH670 3.5 26.8 1.0
C2 A:GOL402 3.6 31.7 0.7
O A:HOH520 3.7 30.0 1.0
C1 A:GOL402 3.8 33.2 0.7
O1 A:GOL402 3.9 36.6 0.7
OD1 A:ASP287 3.9 26.8 1.0
CB A:ASP245 4.0 21.4 1.0
CG A:GLU181 4.1 18.5 1.0
CE1 A:HIS220 4.1 19.6 1.0
CG A:GLU217 4.3 21.1 1.0
CB A:GLU217 4.3 19.9 1.0
OE2 A:GLU217 4.4 25.1 1.0
OD1 A:ASP245 4.5 23.2 1.0
C3 A:GOL402 4.7 32.2 0.7
NE2 A:HIS220 4.7 23.3 1.0
O A:HOH504 4.7 37.4 1.0
ND1 A:HIS220 4.9 22.8 1.0
MN A:MN404 4.9 24.6 1.0
O A:HOH713 4.9 34.2 1.0
CA A:ASP287 4.9 21.6 1.0
ND2 A:ASN215 5.0 22.5 1.0

Reference:

P.Mehrabi, S.Sung, D.Von Stetten, A.Prester, C.E.Hatton, S.Kleine-Dopke, A.Berkes, G.Gore, J.P.Leimkohl, H.Schikora, M.Kollewe, H.Rohde, M.Wilmanns, F.Tellkamp, E.C.Schulz. Millisecond Cryo-Trapping By the Spitrobot Crystal Plunger Simplifies Time-Resolved Crystallography. Nat Commun V. 14 2365 2023.
ISSN: ESSN 2041-1723
PubMed: 37185266
DOI: 10.1038/S41467-023-37834-W
Page generated: Thu Oct 3 19:04:33 2024

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