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Magnesium in PDB 1muw: The 0.86 Angstrom Structure of Xylose Isomerase

Enzymatic activity of The 0.86 Angstrom Structure of Xylose Isomerase

All present enzymatic activity of The 0.86 Angstrom Structure of Xylose Isomerase:
5.3.1.5;

Protein crystallography data

The structure of The 0.86 Angstrom Structure of Xylose Isomerase, PDB code: 1muw was solved by T.D.Fenn, D.Ringe, G.A.Petsko, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 0.86
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 85.906, 92.883, 98.321, 90.00, 90.00, 90.00
R / Rfree (%) 12.5 / 14.3

Other elements in 1muw:

The structure of The 0.86 Angstrom Structure of Xylose Isomerase also contains other interesting chemical elements:

Manganese (Mn) 4 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the The 0.86 Angstrom Structure of Xylose Isomerase (pdb code 1muw). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the The 0.86 Angstrom Structure of Xylose Isomerase, PDB code: 1muw:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 1muw

Go back to Magnesium Binding Sites List in 1muw
Magnesium binding site 1 out of 2 in the The 0.86 Angstrom Structure of Xylose Isomerase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of The 0.86 Angstrom Structure of Xylose Isomerase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg453

b:15.4
occ:1.00
H A:ARG207 2.1 11.4 0.7
H A:ARG207 2.2 12.5 0.3
HA A:ASP162 2.6 8.6 1.0
OD1 A:ASP162 2.7 8.6 1.0
HB3 A:GLU206 2.8 15.2 0.7
OH A:TYR211 2.8 8.7 1.0
O A:HOH829 2.8 14.1 1.0
HE1 A:TYR211 2.8 9.6 1.0
HB2 A:GLU206 2.8 12.8 0.3
H A:GLU206 2.9 10.8 0.7
H A:GLU206 2.9 11.4 0.3
N A:ARG207 2.9 9.5 0.7
HB3 A:LEU205 3.0 8.3 1.0
N A:ARG207 3.0 10.4 0.3
HB2 A:ARG207 3.0 13.4 0.3
HB2 A:ARG207 3.0 13.6 0.7
N A:GLU206 3.3 9.0 0.7
N A:GLU206 3.3 9.5 0.3
HH A:TYR211 3.4 13.0 1.0
CE1 A:TYR211 3.4 8.0 1.0
CZ A:TYR211 3.5 7.9 1.0
HG3 A:ARG207 3.5 14.3 0.7
CA A:ASP162 3.6 7.1 1.0
CB A:GLU206 3.6 12.6 0.7
CB A:GLU206 3.7 10.6 0.3
CG A:ASP162 3.7 7.9 1.0
CB A:ARG207 3.7 11.3 0.7
CA A:GLU206 3.7 11.2 0.7
CA A:GLU206 3.7 10.1 0.3
CB A:ARG207 3.8 11.2 0.3
C A:GLU206 3.8 10.6 0.7
C A:GLU206 3.8 10.5 0.3
CA A:ARG207 3.8 9.9 0.7
CA A:ARG207 3.8 10.5 0.3
HA3 A:GLY165 3.9 10.1 1.0
CB A:LEU205 3.9 7.0 1.0
CB A:ASP162 4.0 7.7 1.0
HB2 A:GLU206 4.0 15.2 0.7
O A:PHE161 4.1 8.0 0.1
HG3 A:ARG207 4.1 15.1 0.3
CG A:ARG207 4.1 11.9 0.7
C A:LEU205 4.2 8.6 1.0
HB3 A:GLU206 4.2 12.8 0.3
HB3 A:ASP162 4.2 9.2 1.0
HD2 A:ARG207 4.2 20.9 0.3
C A:ARG207 4.2 9.6 0.7
O A:ARG207 4.2 8.7 0.7
HB2 A:LEU205 4.2 8.3 1.0
C A:ARG207 4.2 10.3 0.3
O A:ARG207 4.3 11.0 0.3
O A:PHE161 4.3 6.4 0.9
N A:ASP162 4.3 6.5 1.0
HD2 A:ARG207 4.4 18.7 0.7
HD13 A:LEU205 4.4 10.5 1.0
O A:ASP162 4.4 8.5 1.0
CG A:ARG207 4.4 12.6 0.3
HD22 A:LEU205 4.5 11.7 1.0
CA A:LEU205 4.5 7.7 1.0
HG3 A:GLU206 4.5 15.9 0.3
C A:PHE161 4.5 7.1 0.1
C A:ASP162 4.5 7.2 1.0
HB3 A:ARG207 4.5 13.4 0.3
HH11 A:ARG207 4.5 29.0 0.7
HB3 A:ARG207 4.6 13.6 0.7
HA A:LEU205 4.6 9.2 1.0
CD1 A:TYR211 4.6 7.7 1.0
HD11 A:LEU210 4.6 22.4 1.0
C A:PHE161 4.6 6.1 0.9
HG3 A:GLU206 4.6 22.6 0.7
HA A:ARG207 4.7 11.9 0.7
CG A:GLU206 4.7 13.3 0.3
HA A:GLU206 4.7 13.4 0.7
CG A:GLU206 4.7 18.8 0.7
HA A:ARG207 4.7 12.6 0.3
HA A:GLU206 4.7 12.1 0.3
OD2 A:ASP162 4.7 8.9 1.0
CE2 A:TYR211 4.8 7.2 1.0
H A:GLY165 4.8 9.2 1.0
CD A:ARG207 4.8 15.6 0.7
H A:ASP162 4.8 7.8 1.0
CD A:ARG207 4.9 17.4 0.3
CA A:GLY165 4.9 8.4 1.0
HG2 A:ARG207 4.9 14.3 0.7
O A:GLU206 4.9 17.4 0.3
CG A:LEU205 4.9 6.6 1.0
HB3 A:PHE161 4.9 8.6 0.1
HD1 A:TYR211 4.9 9.2 1.0
O A:GLU206 4.9 11.8 0.7
HB2 A:ASP162 5.0 9.2 1.0
HG2 A:GLU206 5.0 22.6 0.7

Magnesium binding site 2 out of 2 in 1muw

Go back to Magnesium Binding Sites List in 1muw
Magnesium binding site 2 out of 2 in the The 0.86 Angstrom Structure of Xylose Isomerase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of The 0.86 Angstrom Structure of Xylose Isomerase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg454

b:23.2
occ:1.00
HD1 A:HIS70 2.2 21.1 1.0
HG2 A:PRO35 2.5 14.5 1.0
O A:LEU57 2.7 11.8 1.0
O A:HOH539 2.7 15.5 1.0
ND1 A:HIS70 2.9 17.6 1.0
HD2 A:PRO35 3.1 12.3 1.0
HB3 A:HIS70 3.2 15.3 1.0
HD13 A:LEU57 3.2 19.4 1.0
O A:HOH866 3.2 39.8 1.0
CG A:PRO35 3.4 12.1 1.0
O A:HOH890 3.4 41.3 1.0
HH11 A:ARG73 3.6 19.6 1.0
CD A:PRO35 3.7 10.2 1.0
CG A:HIS70 3.7 13.6 1.0
HA A:LEU57 3.8 11.2 1.0
C A:LEU57 3.8 9.5 1.0
CB A:HIS70 3.8 12.8 1.0
CE1 A:HIS70 3.8 17.8 1.0
HB2 A:PRO35 3.9 12.2 1.0
HD3 A:PRO35 4.0 12.3 1.0
HE1 A:HIS70 4.0 21.4 1.0
HG3 A:PRO35 4.1 14.5 1.0
HH12 A:ARG73 4.1 19.6 1.0
HA A:HIS70 4.1 15.5 1.0
HD3 A:PRO59 4.1 17.7 1.0
CD1 A:LEU57 4.1 12.9 1.0
NH1 A:ARG73 4.2 16.3 1.0
CB A:PRO35 4.3 10.2 1.0
HD11 A:LEU57 4.3 19.4 1.0
CA A:LEU57 4.3 9.3 1.0
CA A:HIS70 4.5 12.9 1.0
HA A:ILE58 4.5 12.0 1.0
O A:HIS70 4.6 13.4 1.0
HB2 A:HIS70 4.6 15.3 1.0
HD12 A:LEU57 4.7 19.4 1.0
O A:ASP56 4.7 10.5 1.0
HG A:LEU57 4.7 13.1 1.0
HB3 A:PRO35 4.8 12.2 1.0
CD2 A:HIS70 4.8 20.8 1.0
N A:ILE58 4.9 9.5 1.0
NE2 A:HIS70 4.9 18.5 1.0
C A:HIS70 4.9 12.2 1.0
HB2 A:PHE74 4.9 13.0 1.0
N A:PRO35 5.0 9.0 1.0
CG A:LEU57 5.0 10.9 1.0

Reference:

T.D.Fenn, D.Ringe, G.A.Petsko. Active Site Dynamics at 0.86A: Crystallographic Analysis of A Metal-Mediated Hydride Shift To Be Published.
Page generated: Mon Dec 14 06:29:41 2020

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