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Sodium in PDB 1q9i: The A251C:S430C Double Mutant of Flavocytochrome C3 From Shewanella Frigidimarina

Enzymatic activity of The A251C:S430C Double Mutant of Flavocytochrome C3 From Shewanella Frigidimarina

All present enzymatic activity of The A251C:S430C Double Mutant of Flavocytochrome C3 From Shewanella Frigidimarina:
1.3.99.1;

Protein crystallography data

The structure of The A251C:S430C Double Mutant of Flavocytochrome C3 From Shewanella Frigidimarina, PDB code: 1q9i was solved by E.L.Rothery, C.G.Mowat, C.S.Miles, 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) 24.00 / 1.60
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 45.290, 91.885, 78.310, 90.00, 91.50, 90.00
R / Rfree (%) 15.5 / 19.7

Other elements in 1q9i:

The structure of The A251C:S430C Double Mutant of 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 The A251C:S430C Double Mutant of Flavocytochrome C3 From Shewanella Frigidimarina (pdb code 1q9i). 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 The A251C:S430C Double Mutant of Flavocytochrome C3 From Shewanella Frigidimarina, PDB code: 1q9i:

Sodium binding site 1 out of 1 in 1q9i

Go back to Sodium Binding Sites List in 1q9i
Sodium binding site 1 out of 1 in the The A251C:S430C Double Mutant of 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 The A251C:S430C Double Mutant of Flavocytochrome C3 From Shewanella Frigidimarina within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na9810

b:9.4
occ:1.00
 O A:THR506 2.3 8.7 1.0
O A:HOH9826 2.3 10.0 1.0
O A:GLU534 2.4 9.1 1.0
O A:THR536 2.4 10.3 1.0
O A:GLY508 2.4 10.5 1.0
O A:MET507 3.2 10.0 1.0
C A:MET507 3.2 9.1 1.0
O A:HOH9848 3.3 8.7 1.0
C A:GLY508 3.4 10.0 1.0
C A:GLU534 3.4 10.0 1.0
C A:THR506 3.5 9.3 1.0
C A:THR536 3.5 10.2 1.0
N A:GLY508 3.7 9.3 1.0
CA A:MET507 3.7 9.5 1.0
CA A:GLU534 4.0 8.9 1.0
CA A:GLY508 4.0 9.8 1.0
N A:MET507 4.0 9.0 1.0
CG A:GLU534 4.0 9.4 1.0
O A:HOH9818 4.1 11.6 1.0
N A:THR536 4.1 9.6 1.0
O A:HOH9843 4.2 12.5 1.0
C A:VAL535 4.3 8.6 1.0
N A:GLY509 4.3 11.1 1.0
CA A:THR536 4.4 9.3 1.0
N A:GLY537 4.4 9.5 1.0
N A:VAL535 4.4 8.7 1.0
CA A:GLY537 4.6 11.1 1.0
CA A:GLY509 4.6 11.2 1.0
CB A:GLU534 4.6 9.0 1.0
OG1 A:THR506 4.6 9.2 1.0
NE2 A:HIS505 4.7 9.7 1.0
O A:VAL535 4.7 9.5 1.0
CA A:THR506 4.7 8.2 1.0
CA A:VAL535 4.7 9.2 1.0
O A:GLY533 4.8 9.6 1.0
CB A:THR506 4.9 7.4 1.0

Reference:

E.L.Rothery, C.G.Mowat, C.S.Miles, S.Mott, M.D.Walkinshaw, G.A.Reid, S.K.Chapman. Probing Domain Mobility in A Flavocytochrome Biochemistry V. 42 4983 2004.
ISSN: ISSN 0006-2960
PubMed: 15109257
DOI: 10.1021/BI030261W
Page generated: Sun Oct 6 21:24:43 2024

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