Atomistry » Manganese » PDB 4lta-4mu3 » 4lul
Atomistry »
  Manganese »
    PDB 4lta-4mu3 »
      4lul »

Manganese in PDB 4lul: The Crystal Structure of the P132A, Y133D Mutant of Pyrococcus Furiosus Phosphoglucose Isomerase in Complex with Manganese.

Enzymatic activity of The Crystal Structure of the P132A, Y133D Mutant of Pyrococcus Furiosus Phosphoglucose Isomerase in Complex with Manganese.

All present enzymatic activity of The Crystal Structure of the P132A, Y133D Mutant of Pyrococcus Furiosus Phosphoglucose Isomerase in Complex with Manganese.:
5.3.1.9;

Protein crystallography data

The structure of The Crystal Structure of the P132A, Y133D Mutant of Pyrococcus Furiosus Phosphoglucose Isomerase in Complex with Manganese., PDB code: 4lul 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) 25.58 / 1.89
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 41.300, 60.030, 146.670, 90.00, 90.00, 90.00
R / Rfree (%) 19.6 / 25.3

Manganese Binding Sites:

The binding sites of Manganese atom in the The Crystal Structure of the P132A, Y133D Mutant of Pyrococcus Furiosus Phosphoglucose Isomerase in Complex with Manganese. (pdb code 4lul). 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 P132A, Y133D Mutant of Pyrococcus Furiosus Phosphoglucose Isomerase in Complex with Manganese., PDB code: 4lul:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 4lul

Go back to Manganese Binding Sites List in 4lul
Manganese binding site 1 out of 2 in the The Crystal Structure of the P132A, Y133D Mutant of Pyrococcus Furiosus Phosphoglucose Isomerase in Complex with Manganese.


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 P132A, Y133D Mutant of Pyrococcus Furiosus Phosphoglucose Isomerase in Complex with Manganese. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn201

b:30.4
occ:1.00
OE1 A:GLU97 2.1 28.0 1.0
NE2 A:HIS88 2.2 31.9 1.0
O A:HOH307 2.3 30.9 1.0
NE2 A:HIS90 2.3 31.1 1.0
NE2 A:HIS136 2.3 26.9 1.0
O A:HOH324 2.4 31.9 1.0
CD A:GLU97 3.1 26.6 1.0
CD2 A:HIS90 3.1 31.6 1.0
CE1 A:HIS88 3.2 33.3 1.0
CE1 A:HIS136 3.2 25.3 1.0
CD2 A:HIS88 3.3 31.2 1.0
CE1 A:HIS90 3.3 31.5 1.0
CD2 A:HIS136 3.4 26.1 1.0
OE2 A:GLU97 3.4 28.8 1.0
ND1 A:HIS88 4.3 33.2 1.0
CG A:HIS90 4.3 33.5 1.0
O A:HOH330 4.3 49.4 1.0
ND1 A:HIS136 4.4 25.9 1.0
ND1 A:HIS90 4.4 33.5 1.0
CG A:HIS88 4.4 30.7 1.0
OH A:TYR99 4.4 26.4 1.0
CG A:GLU97 4.5 25.2 1.0
CG A:HIS136 4.5 24.8 1.0
CB A:GLU97 4.8 23.1 1.0

Manganese binding site 2 out of 2 in 4lul

Go back to Manganese Binding Sites List in 4lul
Manganese binding site 2 out of 2 in the The Crystal Structure of the P132A, Y133D Mutant of Pyrococcus Furiosus Phosphoglucose Isomerase in Complex with Manganese.


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 P132A, Y133D Mutant of Pyrococcus Furiosus Phosphoglucose Isomerase in Complex with Manganese. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn201

b:36.0
occ:1.00
OE1 B:GLU97 2.1 33.1 1.0
O B:HOH307 2.2 38.6 1.0
NE2 B:HIS88 2.2 34.8 1.0
NE2 B:HIS136 2.2 26.7 1.0
NE2 B:HIS90 2.4 37.8 1.0
O B:HOH351 2.5 46.2 1.0
CE1 B:HIS136 3.1 27.4 1.0
CD B:GLU97 3.1 32.2 1.0
CD2 B:HIS88 3.2 33.0 1.0
CE1 B:HIS88 3.3 34.9 1.0
CD2 B:HIS90 3.3 38.1 1.0
CE1 B:HIS90 3.3 39.0 1.0
CD2 B:HIS136 3.3 27.1 1.0
OE2 B:GLU97 3.5 34.5 1.0
OH B:TYR99 4.2 27.4 1.0
ND1 B:HIS136 4.3 26.8 1.0
CG B:HIS88 4.3 32.6 1.0
ND1 B:HIS88 4.3 33.6 1.0
ND1 B:HIS90 4.4 38.6 1.0
CG B:HIS136 4.4 26.3 1.0
CG B:HIS90 4.4 39.8 1.0
CG B:GLU97 4.4 29.3 1.0
CB B:GLU97 4.7 26.3 1.0
NE2 B:HIS158 4.8 47.1 1.0
CE1 B:TYR99 5.0 25.3 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: Tue Dec 15 04:24:06 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy