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Sodium in PDB 1e39: Flavocytochrome C3 From Shewanella Frigidimarina Histidine 365 Mutated to Alanine

Enzymatic activity of Flavocytochrome C3 From Shewanella Frigidimarina Histidine 365 Mutated to Alanine

All present enzymatic activity of Flavocytochrome C3 From Shewanella Frigidimarina Histidine 365 Mutated to Alanine:
1.3.99.1;

Protein crystallography data

The structure of Flavocytochrome C3 From Shewanella Frigidimarina Histidine 365 Mutated to Alanine, PDB code: 1e39 was solved by M.K.Doherty, S.L.Pealing, C.S.Miles, R.Moysey, P.Taylor, 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) 18.00 / 1.80
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 45.571, 92.172, 78.489, 90.00, 91.08, 90.00
R / Rfree (%) 18.1 / 24.7

Other elements in 1e39:

The structure of Flavocytochrome C3 From Shewanella Frigidimarina Histidine 365 Mutated to Alanine also contains other interesting chemical elements:

Iron (Fe) 4 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Flavocytochrome C3 From Shewanella Frigidimarina Histidine 365 Mutated to Alanine (pdb code 1e39). 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 Flavocytochrome C3 From Shewanella Frigidimarina Histidine 365 Mutated to Alanine, PDB code: 1e39:

Sodium binding site 1 out of 1 in 1e39

Go back to Sodium Binding Sites List in 1e39
Sodium binding site 1 out of 1 in the Flavocytochrome C3 From Shewanella Frigidimarina Histidine 365 Mutated to Alanine


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Flavocytochrome C3 From Shewanella Frigidimarina Histidine 365 Mutated to Alanine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na810

b:32.7
occ:1.00
 O A:THR536 2.3 10.3 1.0
O A:GLU534 2.4 7.5 1.0
O A:GLY508 2.4 8.4 1.0
O A:THR506 2.4 9.0 1.0
O A:HOH2551 2.5 11.2 1.0
O A:MET507 3.0 12.8 1.0
C A:MET507 3.1 14.7 1.0
C A:GLY508 3.3 11.2 1.0
C A:GLU534 3.4 11.6 1.0
C A:THR536 3.4 18.8 1.0
O A:HOH2552 3.5 14.8 1.0
C A:THR506 3.6 12.1 1.0
N A:GLY508 3.6 11.8 1.0
CA A:MET507 3.7 13.2 1.0
CA A:GLY508 4.0 12.8 1.0
CA A:GLU534 4.0 7.8 1.0
N A:THR536 4.1 7.7 1.0
N A:MET507 4.1 11.8 1.0
CG A:GLU534 4.1 9.8 1.0
O A:HOH2575 4.1 15.0 1.0
O A:HOH2553 4.2 14.0 1.0
C A:VAL535 4.2 9.6 1.0
N A:GLY509 4.3 9.4 1.0
N A:GLY537 4.3 12.9 1.0
CA A:THR536 4.4 10.1 1.0
CA A:GLY537 4.4 11.2 1.0
N A:VAL535 4.5 12.1 1.0
CA A:GLY509 4.5 12.0 1.0
O A:VAL535 4.6 13.0 1.0
OG1 A:THR506 4.6 9.9 1.0
CB A:GLU534 4.7 9.1 1.0
CA A:VAL535 4.7 10.7 1.0
NE2 A:HIS505 4.8 10.7 1.0
CA A:THR506 4.8 8.5 1.0
O A:GLY533 4.9 12.0 1.0
CB A:THR506 5.0 10.4 1.0

Reference:

M.K.Doherty, S.L.Pealing, C.S.Miles, R.Moysey, P.Taylor, M.D.Walkinshaw, G.A.Reid, S.K.Chapman. Identification of the Active Site Acid/Base Catalyst in A Bacterial Fumarate Reductase: A Kinetic and Crystallographic Study Biochemistry V. 39 10695 2000.
ISSN: ISSN 0006-2960
PubMed: 10978153
DOI: 10.1021/BI000871L
Page generated: Sun Oct 6 18:19:23 2024

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