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Sodium in PDB 1kss: Crystal Structure of HIS505ALA Mutant Flavocytochrome C3 From Shewanella Frigidimarina

Enzymatic activity of Crystal Structure of HIS505ALA Mutant Flavocytochrome C3 From Shewanella Frigidimarina

All present enzymatic activity of Crystal Structure of HIS505ALA Mutant Flavocytochrome C3 From Shewanella Frigidimarina:
1.3.99.1;

Protein crystallography data

The structure of Crystal Structure of HIS505ALA Mutant Flavocytochrome C3 From Shewanella Frigidimarina, PDB code: 1kss was solved by K.L.Pankhurst, C.G.Mowat, 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) 10.00 / 1.80
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 45.632, 92.798, 79.056, 90.00, 91.02, 90.00
R / Rfree (%) 15.6 / 20.6

Other elements in 1kss:

The structure of Crystal Structure of HIS505ALA Mutant Flavocytochrome C3 From Shewanella Frigidimarina also contains other interesting chemical elements:

Iron (Fe) 4 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of HIS505ALA Mutant Flavocytochrome C3 From Shewanella Frigidimarina (pdb code 1kss). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Crystal Structure of HIS505ALA Mutant Flavocytochrome C3 From Shewanella Frigidimarina, PDB code: 1kss:

Sodium binding site 1 out of 1 in 1kss

Go back to Sodium Binding Sites List in 1kss
Sodium binding site 1 out of 1 in the Crystal Structure of HIS505ALA Mutant Flavocytochrome C3 From Shewanella Frigidimarina


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 HIS505ALA Mutant Flavocytochrome C3 From Shewanella Frigidimarina within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na1810

b:10.7
occ:1.00
 O A:HOH1849 2.5 10.7 1.0
O A:GLU534 2.5 10.1 1.0
O A:THR536 2.5 10.3 1.0
O A:GLY508 2.5 10.7 1.0
O A:THR506 2.6 13.3 1.0
O A:MET507 3.3 13.3 1.0
C A:MET507 3.4 12.9 1.0
O A:HOH1855 3.4 13.0 1.0
C A:GLY508 3.5 12.3 1.0
C A:GLU534 3.5 10.7 1.0
C A:THR536 3.6 12.6 1.0
C A:THR506 3.7 11.6 1.0
N A:GLY508 3.7 13.2 1.0
CA A:MET507 3.8 13.5 1.0
CA A:GLU534 4.0 11.0 1.0
CG A:GLU534 4.1 12.4 1.0
CA A:GLY508 4.1 12.2 1.0
N A:MET507 4.1 12.7 1.0
N A:THR536 4.1 10.8 1.0
C A:VAL535 4.3 10.5 1.0
O A:HOH1970 4.3 15.2 1.0
N A:GLY509 4.4 11.3 1.0
O A:HOH1879 4.4 15.8 1.0
CA A:THR536 4.5 10.8 1.0
N A:GLY537 4.5 11.7 1.0
N A:VAL535 4.5 9.2 1.0
CB A:GLU534 4.6 11.4 1.0
CA A:GLY537 4.6 11.9 1.0
CA A:GLY509 4.6 11.2 1.0
OG1 A:THR506 4.7 11.3 1.0
O A:VAL535 4.7 10.5 1.0
CA A:VAL535 4.7 10.4 1.0
O A:HOH1811 4.8 6.9 1.0
CA A:THR506 4.9 11.6 1.0
O A:GLY533 4.9 11.2 1.0

Reference:

K.L.Pankhurst, C.G.Mowat, C.S.Miles, D.Leys, M.D.Walkinshaw, G.A.Reid, S.K.Chapman. Role of HIS505 in the Soluble Fumarate Reductase From Shewanella Frigidimarina. Biochemistry V. 41 8551 2002.
ISSN: ISSN 0006-2960
PubMed: 12093271
DOI: 10.1021/BI020155E
Page generated: Sun Oct 6 19:39:49 2024

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