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Magnesium in PDB 1pow: The Refined Structures of A Stabilized Mutant and of Wild-Type Pyruvate Oxidase From Lactobacillus Plantarum

Enzymatic activity of The Refined Structures of A Stabilized Mutant and of Wild-Type Pyruvate Oxidase From Lactobacillus Plantarum

All present enzymatic activity of The Refined Structures of A Stabilized Mutant and of Wild-Type Pyruvate Oxidase From Lactobacillus Plantarum:
1.2.3.3;

Protein crystallography data

The structure of The Refined Structures of A Stabilized Mutant and of Wild-Type Pyruvate Oxidase From Lactobacillus Plantarum, PDB code: 1pow was solved by Y.A.Muller, G.E.Schulz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 2.50
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 121.600, 155.400, 167.100, 90.00, 90.00, 90.00
R / Rfree (%) 19.8 / n/a

Magnesium Binding Sites:

The binding sites of Magnesium atom in the The Refined Structures of A Stabilized Mutant and of Wild-Type Pyruvate Oxidase From Lactobacillus Plantarum (pdb code 1pow). 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 Refined Structures of A Stabilized Mutant and of Wild-Type Pyruvate Oxidase From Lactobacillus Plantarum, PDB code: 1pow:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 1pow

Go back to Magnesium Binding Sites List in 1pow
Magnesium binding site 1 out of 2 in the The Refined Structures of A Stabilized Mutant and of Wild-Type Pyruvate Oxidase From Lactobacillus Plantarum


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of The Refined Structures of A Stabilized Mutant and of Wild-Type Pyruvate Oxidase From Lactobacillus Plantarum within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg610

b:2.1
occ:1.00
O3B A:TPP611 1.9 9.7 1.0
O1A A:TPP611 1.9 3.1 1.0
O A:GLN476 2.0 8.2 1.0
OD1 A:ASP447 2.0 2.9 1.0
OD1 A:ASN474 2.0 3.6 1.0
PB A:TPP611 2.9 9.2 1.0
O3A A:TPP611 3.0 2.4 1.0
PA A:TPP611 3.0 4.1 1.0
CG A:ASN474 3.1 3.0 1.0
CG A:ASP447 3.2 2.7 1.0
C A:GLN476 3.2 6.4 1.0
O2B A:TPP611 3.5 7.5 1.0
ND2 A:ASN474 3.5 2.0 1.0
OD2 A:ASP447 3.8 4.7 1.0
O7 A:TPP611 3.8 2.0 1.0
N A:TYR477 4.1 5.0 1.0
N A:GLY448 4.1 4.1 1.0
N A:GLY478 4.1 3.5 1.0
O1B A:TPP611 4.1 9.4 1.0
N A:ASP447 4.1 3.3 1.0
CA A:TYR477 4.2 5.4 1.0
O2A A:TPP611 4.2 4.9 1.0
N A:GLN476 4.3 6.1 1.0
CA A:GLN476 4.3 5.5 1.0
CB A:ASP447 4.4 2.0 1.0
O A:PHE472 4.4 12.3 1.0
CB A:ASN474 4.5 2.0 1.0
CA A:ASP447 4.6 2.0 1.0
C A:TYR477 4.7 4.2 1.0
C A:GLY446 4.7 3.6 1.0
CA A:GLY446 4.7 3.8 1.0
N A:ASN474 4.8 5.1 1.0
CB A:GLN476 4.8 6.5 1.0
CZ A:PHE497 4.8 6.1 1.0
C A:ASP447 4.8 5.8 1.0
CA A:GLY448 5.0 3.1 1.0

Magnesium binding site 2 out of 2 in 1pow

Go back to Magnesium Binding Sites List in 1pow
Magnesium binding site 2 out of 2 in the The Refined Structures of A Stabilized Mutant and of Wild-Type Pyruvate Oxidase From Lactobacillus Plantarum


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of The Refined Structures of A Stabilized Mutant and of Wild-Type Pyruvate Oxidase From Lactobacillus Plantarum within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg610

b:2.1
occ:1.00
O3B B:TPP611 1.9 10.1 1.0
O1A B:TPP611 1.9 2.7 1.0
OD1 B:ASP447 2.0 2.1 1.0
OD1 B:ASN474 2.0 4.6 1.0
O B:GLN476 2.0 4.9 1.0
O3A B:TPP611 2.7 7.3 1.0
PB B:TPP611 2.8 6.2 1.0
PA B:TPP611 2.8 6.5 1.0
CG B:ASN474 3.1 4.3 1.0
CG B:ASP447 3.2 4.1 1.0
C B:GLN476 3.3 3.5 1.0
O2B B:TPP611 3.4 6.4 1.0
ND2 B:ASN474 3.5 2.9 1.0
O7 B:TPP611 3.6 3.2 1.0
OD2 B:ASP447 3.9 4.8 1.0
O2A B:TPP611 4.0 6.6 1.0
N B:ASP447 4.0 4.1 1.0
O1B B:TPP611 4.0 2.1 1.0
N B:GLY478 4.1 2.9 1.0
N B:TYR477 4.2 2.0 1.0
N B:GLY448 4.2 4.4 1.0
CA B:TYR477 4.2 2.0 1.0
N B:GLN476 4.3 2.0 1.0
CA B:GLN476 4.3 2.0 1.0
CB B:ASP447 4.4 3.5 1.0
O B:PHE472 4.4 7.9 1.0
CB B:ASN474 4.5 2.0 1.0
CA B:ASP447 4.6 2.9 1.0
C B:GLY446 4.6 2.3 1.0
CA B:GLY446 4.7 4.4 1.0
C B:TYR477 4.7 2.0 1.0
CZ B:PHE497 4.8 8.1 1.0
CB B:GLN476 4.8 2.5 1.0
N B:ASN474 4.8 7.4 1.0
C B:ASP447 4.9 2.0 1.0

Reference:

Y.A.Muller, G.Schumacher, R.Rudolph, G.E.Schulz. The Refined Structures of A Stabilized Mutant and of Wild-Type Pyruvate Oxidase From Lactobacillus Plantarum. J.Mol.Biol. V. 237 315 1994.
ISSN: ISSN 0022-2836
PubMed: 8145244
DOI: 10.1006/JMBI.1994.1233
Page generated: Tue Aug 13 10:53:42 2024

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