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Manganese in PDB 4lum: The Crystal Structure of the P132V Mutant of Pyrococcus Furiosus Phosphoglucose Isomerase in Complex with Manganese and Fructose-6- Phosphate.

Enzymatic activity of The Crystal Structure of the P132V Mutant of Pyrococcus Furiosus Phosphoglucose Isomerase in Complex with Manganese and Fructose-6- Phosphate.

All present enzymatic activity of The Crystal Structure of the P132V Mutant of Pyrococcus Furiosus Phosphoglucose Isomerase in Complex with Manganese and Fructose-6- Phosphate.:
5.3.1.9;

Protein crystallography data

The structure of The Crystal Structure of the P132V Mutant of Pyrococcus Furiosus Phosphoglucose Isomerase in Complex with Manganese and Fructose-6- Phosphate., PDB code: 4lum was solved by P.J.Baker, F.M.Almourfi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 18.49 / 1.79
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 44.940, 45.010, 48.690, 87.81, 89.86, 75.47
R / Rfree (%) 17.3 / 22

Manganese Binding Sites:

The binding sites of Manganese atom in the The Crystal Structure of the P132V Mutant of Pyrococcus Furiosus Phosphoglucose Isomerase in Complex with Manganese and Fructose-6- Phosphate. (pdb code 4lum). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the The Crystal Structure of the P132V Mutant of Pyrococcus Furiosus Phosphoglucose Isomerase in Complex with Manganese and Fructose-6- Phosphate., PDB code: 4lum:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 4lum

Go back to Manganese Binding Sites List in 4lum
Manganese binding site 1 out of 2 in the The Crystal Structure of the P132V Mutant of Pyrococcus Furiosus Phosphoglucose Isomerase in Complex with Manganese and Fructose-6- Phosphate.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of The Crystal Structure of the P132V Mutant of Pyrococcus Furiosus Phosphoglucose Isomerase in Complex with Manganese and Fructose-6- Phosphate. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn201

b:19.0
occ:1.00
OE1 A:GLU97 2.1 24.1 1.0
O1 A:F6R202 2.2 24.6 1.0
O2 A:F6R202 2.2 22.9 1.0
NE2 A:HIS136 2.3 15.3 1.0
NE2 A:HIS88 2.3 16.0 1.0
NE2 A:HIS90 2.3 19.1 1.0
C2 A:F6R202 3.0 26.7 1.0
CD A:GLU97 3.1 22.9 1.0
C1 A:F6R202 3.1 27.2 1.0
CE1 A:HIS88 3.2 16.7 1.0
CD2 A:HIS90 3.2 19.7 1.0
CE1 A:HIS136 3.2 14.8 1.0
CD2 A:HIS136 3.3 14.0 1.0
CE1 A:HIS90 3.3 19.3 1.0
CD2 A:HIS88 3.4 14.7 1.0
OE2 A:GLU97 3.4 25.8 1.0
ND1 A:HIS88 4.3 17.0 1.0
CG A:HIS90 4.4 19.5 1.0
ND1 A:HIS136 4.4 14.7 1.0
ND1 A:HIS90 4.4 19.2 1.0
OH A:TYR99 4.4 19.4 1.0
CG A:HIS136 4.4 13.0 1.0
CG A:HIS88 4.4 15.1 1.0
O A:HOH335 4.5 26.6 1.0
CG A:GLU97 4.5 18.9 1.0
C3 A:F6R202 4.5 26.2 1.0
CB A:GLU97 4.7 17.4 1.0
NE2 A:HIS158 5.0 29.2 1.0

Manganese binding site 2 out of 2 in 4lum

Go back to Manganese Binding Sites List in 4lum
Manganese binding site 2 out of 2 in the The Crystal Structure of the P132V Mutant of Pyrococcus Furiosus Phosphoglucose Isomerase in Complex with Manganese and Fructose-6- Phosphate.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of The Crystal Structure of the P132V Mutant of Pyrococcus Furiosus Phosphoglucose Isomerase in Complex with Manganese and Fructose-6- Phosphate. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn201

b:26.4
occ:1.00
OE1 B:GLU97 2.1 30.3 1.0
NE2 B:HIS136 2.2 23.1 1.0
O1 B:F6R202 2.3 30.2 1.0
O2 B:F6R202 2.3 26.0 1.0
NE2 B:HIS90 2.3 27.0 1.0
NE2 B:HIS88 2.3 24.8 1.0
C2 B:F6R202 3.1 28.1 1.0
C1 B:F6R202 3.2 28.8 1.0
CE1 B:HIS136 3.2 22.8 1.0
CD2 B:HIS90 3.2 27.8 1.0
CD B:GLU97 3.2 28.8 1.0
CE1 B:HIS88 3.2 24.7 1.0
CD2 B:HIS136 3.3 21.6 1.0
CE1 B:HIS90 3.3 27.6 1.0
CD2 B:HIS88 3.4 25.0 1.0
OE2 B:GLU97 3.5 32.9 1.0
OH B:TYR99 4.3 25.5 1.0
ND1 B:HIS136 4.3 22.5 1.0
CG B:HIS90 4.3 28.5 1.0
ND1 B:HIS88 4.3 24.5 1.0
ND1 B:HIS90 4.4 28.1 1.0
CG B:HIS136 4.4 21.6 1.0
CG B:HIS88 4.5 24.4 1.0
C3 B:F6R202 4.5 28.1 1.0
O B:HOH367 4.5 43.6 1.0
CG B:GLU97 4.5 25.1 1.0
CD2 B:HIS158 4.7 42.5 1.0
NE2 B:HIS158 4.8 43.7 1.0
CB B:GLU97 4.8 23.0 1.0
C4 B:F6R202 5.0 27.4 1.0

Reference:

P.J.Baker, F.M.Almourfi, J.Raedts, H-J.Joosten, S.Hendriks, S.W.M.Kengen, W.R.Hage, P.J.Schaap, S.E.Sedelnikova, J.Van Der Oost. Correlated Mutation Analysis As A Tool For Smart Library Design to Improve Protein Performance. To Be Published.
Page generated: Sat Oct 5 20:16:42 2024

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