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Sodium in PDB 2fsu: Crystal Structure of the Phnh Protein From Escherichia Coli

Protein crystallography data

The structure of Crystal Structure of the Phnh Protein From Escherichia Coli, PDB code: 2fsu was solved by M.A.Adams, Y.Luo, D.L.Zechel, Z.Jia, Montreal-Kingston Bacterialstructural Genomics Initiative (Bsgi), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.92 / 1.70
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 53.020, 87.418, 75.890, 90.00, 90.00, 90.00
R / Rfree (%) 18.8 / 24.8

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of the Phnh Protein From Escherichia Coli (pdb code 2fsu). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 4 binding sites of Sodium where determined in the Crystal Structure of the Phnh Protein From Escherichia Coli, PDB code: 2fsu:
Jump to Sodium binding site number: 1; 2; 3; 4;

Sodium binding site 1 out of 4 in 2fsu

Go back to Sodium Binding Sites List in 2fsu
Sodium binding site 1 out of 4 in the Crystal Structure of the Phnh Protein From Escherichia Coli


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 the Phnh Protein From Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na501

b:26.2
occ:0.50
O A:HOH509 2.9 21.2 1.0
O A:HOH638 3.6 31.2 1.0
O A:LEU153 3.8 16.3 1.0
CB A:GLN152 3.9 14.0 1.0
N A:LEU153 4.0 15.7 1.0
CA A:GLN152 4.2 14.4 1.0
OE1 A:GLN152 4.3 22.7 1.0
C A:GLN152 4.4 13.7 1.0
C A:LEU153 4.4 14.7 1.0
CG A:GLN152 4.5 17.8 1.0
O A:HOH510 4.8 28.4 1.0
CD A:GLN152 4.9 22.8 1.0
CA A:LEU153 4.9 13.9 1.0
OE1 A:GLU99 4.9 36.1 1.0

Sodium binding site 2 out of 4 in 2fsu

Go back to Sodium Binding Sites List in 2fsu
Sodium binding site 2 out of 4 in the Crystal Structure of the Phnh Protein From Escherichia Coli


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 the Phnh Protein From Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na503

b:35.8
occ:1.00
O A:HOH668 2.6 24.6 1.0
O A:HOH540 2.7 20.3 1.0
CZ A:PHE94 3.6 17.5 1.0
CG2 A:THR93 3.8 18.1 1.0
CE1 A:PHE94 3.9 21.8 1.0
O A:HOH642 3.9 31.9 1.0
O A:HOH548 4.0 37.6 1.0
OG1 A:THR122 4.5 16.6 1.0
CE2 A:PHE94 4.5 16.6 1.0
O A:HOH541 4.7 60.2 1.0
CD1 A:PHE94 5.0 19.7 1.0

Sodium binding site 3 out of 4 in 2fsu

Go back to Sodium Binding Sites List in 2fsu
Sodium binding site 3 out of 4 in the Crystal Structure of the Phnh Protein From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 3 of Crystal Structure of the Phnh Protein From Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na504

b:38.3
occ:1.00
O A:HOH584 2.6 22.6 1.0
O A:HOH589 3.8 40.8 1.0
CB A:PRO67 4.0 19.9 1.0
OD2 A:ASP98 4.3 18.5 1.0
O A:HOH572 4.5 24.2 1.0
CG A:PRO67 4.6 22.7 1.0

Sodium binding site 4 out of 4 in 2fsu

Go back to Sodium Binding Sites List in 2fsu
Sodium binding site 4 out of 4 in the Crystal Structure of the Phnh Protein From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 4 of Crystal Structure of the Phnh Protein From Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na505

b:54.7
occ:0.50
O A:MSE25 3.6 26.0 0.5
C A:MSE25 3.7 25.8 0.5
N A:SER26 3.8 26.4 1.0
CB A:MSE25 3.8 25.7 0.5
CB A:MSE25 3.8 24.6 0.5
OG A:SER26 3.9 33.2 1.0
O A:HOH636 3.9 41.0 1.0
C A:MSE25 3.9 25.6 0.5
CA A:SER26 4.0 28.9 1.0
O A:MSE25 4.2 22.7 0.5
O A:HOH576 4.2 32.4 1.0
O A:HOH662 4.2 42.6 1.0
CA A:MSE25 4.4 24.6 0.5
CA A:MSE25 4.5 25.0 0.5
CB A:SER26 4.6 29.8 1.0
O A:LEU22 4.9 26.1 1.0
CE A:MSE25 5.0 30.5 0.5
CG A:MSE25 5.0 28.1 0.5

Reference:

M.A.Adams, Y.Luo, B.Hove-Jensen, S.M.He, L.M.Van Staalduinen, D.L.Zechel, Z.Jia. Crystal Structure of Phnh: An Essential Component of Carbon-Phosphorus Lyase in Escherichia Coli. J.Bacteriol. V. 190 1072 2008.
ISSN: ISSN 0021-9193
PubMed: 17993513
DOI: 10.1128/JB.01274-07
Page generated: Tue Dec 15 05:49:12 2020

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