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Manganese in PDB 1nfz: Structure and Mechanism of Action of Isopentenylpyrophosphate- Dimethylallylpyrophosphate Isomerase: Complex with Eipp

Enzymatic activity of Structure and Mechanism of Action of Isopentenylpyrophosphate- Dimethylallylpyrophosphate Isomerase: Complex with Eipp

All present enzymatic activity of Structure and Mechanism of Action of Isopentenylpyrophosphate- Dimethylallylpyrophosphate Isomerase: Complex with Eipp:
5.3.3.2;

Protein crystallography data

The structure of Structure and Mechanism of Action of Isopentenylpyrophosphate- Dimethylallylpyrophosphate Isomerase: Complex with Eipp, PDB code: 1nfz was solved by J.Wouters, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.97
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 69.100, 72.110, 91.520, 90.00, 90.00, 90.00
R / Rfree (%) 18.1 / 23.7

Other elements in 1nfz:

The structure of Structure and Mechanism of Action of Isopentenylpyrophosphate- Dimethylallylpyrophosphate Isomerase: Complex with Eipp also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms

Manganese Binding Sites:

The binding sites of Manganese atom in the Structure and Mechanism of Action of Isopentenylpyrophosphate- Dimethylallylpyrophosphate Isomerase: Complex with Eipp (pdb code 1nfz). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Structure and Mechanism of Action of Isopentenylpyrophosphate- Dimethylallylpyrophosphate Isomerase: Complex with Eipp, PDB code: 1nfz:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 1nfz

Go back to Manganese Binding Sites List in 1nfz
Manganese binding site 1 out of 2 in the Structure and Mechanism of Action of Isopentenylpyrophosphate- Dimethylallylpyrophosphate Isomerase: Complex with Eipp


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Structure and Mechanism of Action of Isopentenylpyrophosphate- Dimethylallylpyrophosphate Isomerase: Complex with Eipp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn201

b:20.4
occ:1.00
NE2 A:HIS25 2.1 22.7 1.0
OE2 A:GLU116 2.1 20.4 1.0
OE2 A:GLU114 2.1 20.9 1.0
NE2 A:HIS32 2.1 29.6 1.0
NE2 A:HIS69 2.2 27.5 1.0
OE1 A:GLU114 2.2 22.9 1.0
CD A:GLU114 2.5 27.1 1.0
CE1 A:HIS25 3.0 26.9 1.0
CE1 A:HIS32 3.0 30.0 1.0
CD2 A:HIS25 3.1 22.5 1.0
CD2 A:HIS69 3.1 26.0 1.0
CE1 A:HIS69 3.1 28.3 1.0
CD A:GLU116 3.1 27.2 1.0
CD2 A:HIS32 3.2 29.2 1.0
CG A:GLU116 3.7 25.6 1.0
CG A:GLU114 4.0 24.3 1.0
ND1 A:HIS25 4.1 26.1 1.0
ND1 A:HIS32 4.2 27.4 1.0
OE1 A:GLU116 4.2 23.5 1.0
CG A:HIS25 4.2 25.0 1.0
ND1 A:HIS69 4.3 23.5 1.0
O A:HOH506 4.3 23.8 1.0
CG A:HIS69 4.3 25.6 1.0
CG A:HIS32 4.3 26.4 1.0
C10 A:EIP301 4.4 35.5 1.0
O15 A:EIP301 4.7 68.9 1.0
C11 A:EIP301 4.8 43.5 1.0
CB A:GLU114 4.8 23.4 1.0

Manganese binding site 2 out of 2 in 1nfz

Go back to Manganese Binding Sites List in 1nfz
Manganese binding site 2 out of 2 in the Structure and Mechanism of Action of Isopentenylpyrophosphate- Dimethylallylpyrophosphate Isomerase: Complex with Eipp


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Structure and Mechanism of Action of Isopentenylpyrophosphate- Dimethylallylpyrophosphate Isomerase: Complex with Eipp within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn201

b:25.1
occ:1.00
NE2 B:HIS25 2.0 25.9 1.0
NE2 B:HIS32 2.0 28.4 1.0
NE2 B:HIS69 2.1 28.1 1.0
OE2 B:GLU116 2.1 23.8 1.0
OE2 B:GLU114 2.2 24.6 1.0
OE1 B:GLU114 2.4 22.2 1.0
CD B:GLU114 2.6 25.4 1.0
CE1 B:HIS25 2.9 30.0 1.0
CE1 B:HIS32 3.0 30.9 1.0
CD2 B:HIS69 3.1 26.8 1.0
CE1 B:HIS69 3.1 29.5 1.0
CD2 B:HIS32 3.1 27.8 1.0
CD2 B:HIS25 3.1 27.1 1.0
CD B:GLU116 3.2 26.8 1.0
CG B:GLU116 3.8 25.5 1.0
CG B:GLU114 4.1 25.7 1.0
ND1 B:HIS25 4.1 29.8 1.0
ND1 B:HIS32 4.1 29.5 1.0
OE1 B:GLU116 4.2 22.5 1.0
ND1 B:HIS69 4.2 26.3 1.0
CG B:HIS25 4.2 26.2 1.0
CG B:HIS69 4.2 26.1 1.0
CG B:HIS32 4.2 26.9 1.0
O B:HOH774 4.4 41.0 1.0
C10 B:EIP302 4.6 36.6 1.0
C11 B:EIP302 4.9 46.1 1.0
CG1 B:VAL6 5.0 28.9 1.0
O15 B:EIP302 5.0 60.4 1.0
CB B:GLU114 5.0 23.9 1.0

Reference:

J.Wouters, Y.Oudjama, S.J.Barkley, C.Tricot, V.Stalon, L.Droogmans, C.D.Poulter. Catalytic Mechanism of Escherichia Coli Isopentenyl Diphosphate Isomerase Involves Cys-67, Glu-116, and Tyr-104 As Suggested By Crystal Structures of Complexes with Transition State Analogues and Irreversible Inhibitors J.Biol.Chem. V. 278 11903 2003.
ISSN: ISSN 0021-9258
PubMed: 12540835
DOI: 10.1074/JBC.M212823200
Page generated: Sat Oct 5 11:52:04 2024

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