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Manganese in PDB 4lta: The Crystal Structure of the P132R, Y133G Mutant of Pyrococcus Furiosus Phosphoglucose Isomerase in Complex with Manganese and 5- Phospho-D-Arabinonate.

Enzymatic activity of The Crystal Structure of the P132R, Y133G Mutant of Pyrococcus Furiosus Phosphoglucose Isomerase in Complex with Manganese and 5- Phospho-D-Arabinonate.

All present enzymatic activity of The Crystal Structure of the P132R, Y133G Mutant of Pyrococcus Furiosus Phosphoglucose Isomerase in Complex with Manganese and 5- Phospho-D-Arabinonate.:
5.3.1.9;

Protein crystallography data

The structure of The Crystal Structure of the P132R, Y133G Mutant of Pyrococcus Furiosus Phosphoglucose Isomerase in Complex with Manganese and 5- Phospho-D-Arabinonate., PDB code: 4lta 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) 26.58 / 2.04
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 72.950, 74.470, 75.900, 90.00, 90.00, 90.00
R / Rfree (%) 21.7 / 29.5

Manganese Binding Sites:

The binding sites of Manganese atom in the The Crystal Structure of the P132R, Y133G Mutant of Pyrococcus Furiosus Phosphoglucose Isomerase in Complex with Manganese and 5- Phospho-D-Arabinonate. (pdb code 4lta). 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 P132R, Y133G Mutant of Pyrococcus Furiosus Phosphoglucose Isomerase in Complex with Manganese and 5- Phospho-D-Arabinonate., PDB code: 4lta:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 4lta

Go back to Manganese Binding Sites List in 4lta
Manganese binding site 1 out of 2 in the The Crystal Structure of the P132R, Y133G Mutant of Pyrococcus Furiosus Phosphoglucose Isomerase in Complex with Manganese and 5- Phospho-D-Arabinonate.


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 P132R, Y133G Mutant of Pyrococcus Furiosus Phosphoglucose Isomerase in Complex with Manganese and 5- Phospho-D-Arabinonate. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn201

b:26.4
occ:1.00
O1A A:PA5202 2.2 15.0 1.0
NE2 A:HIS90 2.2 19.2 1.0
OE1 A:GLU97 2.2 24.8 1.0
NE2 A:HIS136 2.4 32.0 1.0
NE2 A:HIS88 2.5 29.2 1.0
O A:HOH357 2.7 32.4 1.0
C1 A:PA5202 3.1 0.6 1.0
CD2 A:HIS90 3.1 20.9 1.0
CD A:GLU97 3.2 63.4 1.0
CE1 A:HIS136 3.2 31.6 1.0
CE1 A:HIS90 3.2 20.8 1.0
O1 A:PA5202 3.3 32.9 1.0
CD2 A:HIS88 3.4 23.5 1.0
CE1 A:HIS88 3.5 44.2 1.0
CD2 A:HIS136 3.5 23.5 1.0
OE2 A:GLU97 3.5 42.8 1.0
CG A:HIS90 4.3 15.9 1.0
ND1 A:HIS90 4.3 20.9 1.0
ND1 A:HIS136 4.4 24.1 1.0
C2 A:PA5202 4.5 45.5 1.0
CG A:HIS136 4.6 14.8 1.0
ND1 A:HIS88 4.6 32.5 1.0
OH A:TYR99 4.6 26.5 1.0
NE2 A:HIS158 4.6 36.4 1.0
CG A:HIS88 4.6 47.0 1.0
CG A:GLU97 4.6 30.2 1.0
CD2 A:HIS158 4.8 83.7 1.0
CB A:GLU97 4.9 17.3 1.0
O3 A:PA5202 4.9 38.2 1.0
C3 A:PA5202 5.0 28.7 1.0

Manganese binding site 2 out of 2 in 4lta

Go back to Manganese Binding Sites List in 4lta
Manganese binding site 2 out of 2 in the The Crystal Structure of the P132R, Y133G Mutant of Pyrococcus Furiosus Phosphoglucose Isomerase in Complex with Manganese and 5- Phospho-D-Arabinonate.


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 P132R, Y133G Mutant of Pyrococcus Furiosus Phosphoglucose Isomerase in Complex with Manganese and 5- Phospho-D-Arabinonate. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn201

b:27.4
occ:1.00
NE2 B:HIS90 2.2 24.2 1.0
O1 B:PA5202 2.3 25.9 1.0
O B:HOH380 2.3 26.2 1.0
OE1 B:GLU97 2.3 27.4 1.0
NE2 B:HIS136 2.3 83.1 1.0
NE2 B:HIS88 2.3 32.6 1.0
CE1 B:HIS136 2.7 27.9 1.0
C1 B:PA5202 3.2 32.4 1.0
CE1 B:HIS90 3.2 26.0 1.0
CD2 B:HIS90 3.2 16.3 1.0
CE1 B:HIS88 3.2 25.7 1.0
CD B:GLU97 3.3 0.2 1.0
O1A B:PA5202 3.4 58.3 1.0
CD2 B:HIS88 3.4 43.5 1.0
OE2 B:GLU97 3.6 33.2 1.0
CD2 B:HIS136 3.6 26.0 1.0
ND1 B:HIS136 4.0 30.5 1.0
ND1 B:HIS90 4.3 23.7 1.0
CG B:HIS90 4.3 28.6 1.0
ND1 B:HIS88 4.4 55.0 1.0
OH B:TYR99 4.4 30.6 1.0
CG B:HIS88 4.5 30.0 1.0
CG B:HIS136 4.5 55.4 1.0
C2 B:PA5202 4.6 26.6 1.0
CG B:GLU97 4.6 37.2 1.0
CD2 B:HIS158 5.0 44.0 1.0
NE2 B:HIS158 5.0 41.8 1.0
CB B:GLU97 5.0 23.1 1.0
CE1 B:TYR99 5.0 24.8 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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