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Sodium in PDB 2fpr: Crystal Structure the N-Terminal Domain of E. Coli Hisb. Apo Mg Model.

Enzymatic activity of Crystal Structure the N-Terminal Domain of E. Coli Hisb. Apo Mg Model.

All present enzymatic activity of Crystal Structure the N-Terminal Domain of E. Coli Hisb. Apo Mg Model.:
3.1.3.15;

Protein crystallography data

The structure of Crystal Structure the N-Terminal Domain of E. Coli Hisb. Apo Mg Model., PDB code: 2fpr was solved by E.S.Rangarajan, M.Cygler, A.Matte, 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) 50.00 / 1.70
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 53.256, 131.962, 106.140, 90.00, 90.00, 90.00
R / Rfree (%) 18.9 / 22

Other elements in 2fpr:

The structure of Crystal Structure the N-Terminal Domain of E. Coli Hisb. Apo Mg Model. also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms
Zinc (Zn) 2 atoms
Bromine (Br) 7 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure the N-Terminal Domain of E. Coli Hisb. Apo Mg Model. (pdb code 2fpr). 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 the N-Terminal Domain of E. Coli Hisb. Apo Mg Model., PDB code: 2fpr:

Sodium binding site 1 out of 1 in 2fpr

Go back to Sodium Binding Sites List in 2fpr
Sodium binding site 1 out of 1 in the Crystal Structure the N-Terminal Domain of E. Coli Hisb. Apo Mg Model.


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure the N-Terminal Domain of E. Coli Hisb. Apo Mg Model. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Na505

b:10.2
occ:1.00
 O B:PHE23 2.2 10.7 1.0
OD2 B:ASP12 2.4 11.7 1.0
OE2 B:GLU18 2.5 11.7 1.0
O B:HOH554 2.5 11.3 1.0
O B:HOH584 2.5 13.6 1.0
O B:HOH568 2.6 17.7 1.0
CG B:ASP12 3.3 9.2 1.0
C B:PHE23 3.4 9.7 1.0
O B:HOH529 3.5 15.8 1.0
CD B:GLU18 3.6 11.6 1.0
CB B:ASP12 3.7 7.5 1.0
O B:HOH513 4.0 11.5 1.0
CG B:GLU18 4.0 10.4 1.0
CB B:PHE23 4.1 10.1 1.0
O B:HOH569 4.3 16.0 1.0
CA B:PHE23 4.3 9.8 1.0
O B:ASN56 4.3 11.1 1.0
OD1 B:ASP12 4.4 8.8 1.0
N B:GLN24 4.4 9.4 1.0
CA B:GLN24 4.4 9.2 1.0
OE1 B:GLN57 4.5 9.0 1.0
NE2 B:GLN57 4.6 8.2 1.0
OE1 B:GLU18 4.7 11.5 1.0
O B:HOH772 4.8 9.3 1.0
CD B:GLN57 4.8 10.1 1.0
O B:HOH746 4.9 36.8 1.0
O B:HOH551 4.9 14.7 1.0
O B:HOH518 5.0 11.1 1.0

Reference:

E.S.Rangarajan, A.Proteau, J.Wagner, M.N.Hung, A.Matte, M.Cygler. Structural Snapshots of Escherichia Coli Histidinol Phosphate Phosphatase Along the Reaction Pathway. J.Biol.Chem. V. 281 37930 2006.
ISSN: ISSN 0021-9258
PubMed: 16966333
DOI: 10.1074/JBC.M604916200
Page generated: Mon Oct 7 02:29:10 2024

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