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Sodium in PDB 1lj1: Crystal Structure of Q363F/R402A Mutant Flavocytochrome C3

Enzymatic activity of Crystal Structure of Q363F/R402A Mutant Flavocytochrome C3

All present enzymatic activity of Crystal Structure of Q363F/R402A Mutant Flavocytochrome C3:
1.3.99.1;

Protein crystallography data

The structure of Crystal Structure of Q363F/R402A Mutant Flavocytochrome C3, PDB code: 1lj1 was solved by C.G.Mowat, K.L.Pankhurst, C.S.Miles, D.Leys, M.D.Walkinshaw, G.A.Reid, S.K.Chapman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 15.00 / 2.00
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 77.971, 88.280, 90.087, 90.00, 103.89, 90.00
R / Rfree (%) 16.1 / 23.5

Other elements in 1lj1:

The structure of Crystal Structure of Q363F/R402A Mutant Flavocytochrome C3 also contains other interesting chemical elements:

Iron (Fe) 8 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of Q363F/R402A Mutant Flavocytochrome C3 (pdb code 1lj1). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Crystal Structure of Q363F/R402A Mutant Flavocytochrome C3, PDB code: 1lj1:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in 1lj1

Go back to Sodium Binding Sites List in 1lj1
Sodium binding site 1 out of 2 in the Crystal Structure of Q363F/R402A Mutant Flavocytochrome C3


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of Q363F/R402A Mutant Flavocytochrome C3 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na810

b:20.9
occ:1.00
O A:THR536 2.5 9.8 1.0
O A:HOH1722 2.5 10.0 1.0
O A:THR506 2.5 8.0 1.0
O A:GLU534 2.5 9.2 1.0
O A:GLY508 2.7 9.3 1.0
O A:MET507 3.1 9.6 1.0
C A:MET507 3.3 10.8 1.0
C A:GLY508 3.4 11.3 1.0
O A:HOH1707 3.5 12.0 1.0
C A:GLU534 3.5 11.3 1.0
C A:THR506 3.6 10.6 1.0
C A:THR536 3.6 12.9 1.0
N A:GLY508 3.7 10.3 1.0
CA A:MET507 3.7 11.1 1.0
CA A:GLU534 4.0 8.9 1.0
CA A:GLY508 4.0 9.8 1.0
O A:HOH1780 4.1 15.0 1.0
N A:MET507 4.1 11.7 1.0
CG A:GLU534 4.1 9.9 1.0
O A:HOH1802 4.1 14.3 1.0
N A:THR536 4.2 12.3 1.0
C A:VAL535 4.3 12.2 1.0
N A:GLY509 4.4 10.4 1.0
N A:VAL535 4.5 10.1 1.0
CA A:THR536 4.5 11.9 1.0
N A:GLY537 4.5 12.5 1.0
CA A:GLY537 4.5 15.2 1.0
CB A:GLU534 4.6 9.9 1.0
CA A:GLY509 4.6 12.9 1.0
OG1 A:THR506 4.7 10.8 1.0
NE2 A:HIS505 4.7 9.8 1.0
O A:VAL535 4.7 11.5 1.0
CA A:VAL535 4.8 12.1 1.0
CA A:THR506 4.8 9.4 1.0
O A:GLY533 4.9 11.6 1.0

Sodium binding site 2 out of 2 in 1lj1

Go back to Sodium Binding Sites List in 1lj1
Sodium binding site 2 out of 2 in the Crystal Structure of Q363F/R402A Mutant Flavocytochrome C3


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of Crystal Structure of Q363F/R402A Mutant Flavocytochrome C3 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Na810

b:16.1
occ:1.00
O B:GLU534 2.5 10.7 1.0
O B:THR536 2.5 10.4 1.0
O B:THR506 2.5 9.0 1.0
O B:HOH1818 2.5 10.1 1.0
O B:GLY508 2.6 11.4 1.0
O B:MET507 3.1 12.4 1.0
C B:MET507 3.3 12.5 1.0
C B:GLU534 3.4 11.0 1.0
C B:GLY508 3.5 13.6 1.0
O B:HOH1850 3.5 13.4 1.0
C B:THR536 3.6 13.0 1.0
C B:THR506 3.6 11.2 1.0
N B:GLY508 3.7 13.3 1.0
CA B:MET507 3.8 12.2 1.0
CA B:GLU534 3.9 9.4 1.0
O B:HOH1849 3.9 11.2 1.0
CG B:GLU534 4.0 8.2 1.0
O B:HOH1847 4.1 10.0 1.0
N B:THR536 4.1 10.6 1.0
CA B:GLY508 4.1 13.3 1.0
N B:MET507 4.1 11.0 1.0
C B:VAL535 4.3 11.4 1.0
N B:GLY509 4.4 12.3 1.0
N B:VAL535 4.4 8.4 1.0
N B:GLY537 4.5 13.2 1.0
CA B:THR536 4.5 11.3 1.0
CA B:GLY537 4.5 13.4 1.0
CB B:GLU534 4.6 10.0 1.0
CA B:GLY509 4.6 12.7 1.0
OG1 B:THR506 4.7 11.8 1.0
CA B:VAL535 4.7 9.5 1.0
O B:VAL535 4.7 12.8 1.0
NE2 B:HIS505 4.8 11.1 1.0
CA B:THR506 4.9 10.3 1.0
O B:GLY533 4.9 13.7 1.0

Reference:

C.G.Mowat, K.L.Pankhurst, C.S.Miles, D.Leys, M.D.Walkinshaw, G.A.Reid, S.K.Chapman. Engineering Water to Act As the Active Site Acid Catalyst in A Soluble Fumarate Reductase Biochemistry V. 41 11990 2002.
ISSN: ISSN 0006-2960
PubMed: 12356299
DOI: 10.1021/BI0203177
Page generated: Tue Dec 15 05:29:24 2020

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