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Sodium in PDB 3lnt: Crystal Structure of Phosphoglyceromutase From Burkholderia Pseudomallei 1710B with Bound Malonic Acid

Enzymatic activity of Crystal Structure of Phosphoglyceromutase From Burkholderia Pseudomallei 1710B with Bound Malonic Acid

All present enzymatic activity of Crystal Structure of Phosphoglyceromutase From Burkholderia Pseudomallei 1710B with Bound Malonic Acid:
5.4.2.1;

Protein crystallography data

The structure of Crystal Structure of Phosphoglyceromutase From Burkholderia Pseudomallei 1710B with Bound Malonic Acid, PDB code: 3lnt was solved by Seattle Structural Genomics Center For Infectious Disease (Ssgcid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.34 / 2.10
Space group P 65
Cell size a, b, c (Å), α, β, γ (°) 119.620, 119.620, 103.670, 90.00, 90.00, 120.00
R / Rfree (%) 17 / 19.6

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of Phosphoglyceromutase From Burkholderia Pseudomallei 1710B with Bound Malonic Acid (pdb code 3lnt). 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 Phosphoglyceromutase From Burkholderia Pseudomallei 1710B with Bound Malonic Acid, PDB code: 3lnt:

Sodium binding site 1 out of 1 in 3lnt

Go back to Sodium Binding Sites List in 3lnt
Sodium binding site 1 out of 1 in the Crystal Structure of Phosphoglyceromutase From Burkholderia Pseudomallei 1710B with Bound Malonic Acid


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 Phosphoglyceromutase From Burkholderia Pseudomallei 1710B with Bound Malonic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na250

b:27.2
occ:1.00
 O A:HOH284 2.6 25.2 1.0
O A:HOH252 2.7 15.1 1.0
O A:HOH259 2.8 17.3 1.0
O A:HOH281 3.1 28.6 1.0
CB A:TRP23 3.7 15.1 1.0
O A:ARG130 3.8 20.1 1.0
CE2 A:TYR138 3.8 14.4 1.0
O A:TRP23 3.9 17.2 1.0
CE3 A:TRP23 4.0 13.2 1.0
CB A:PRO132 4.0 18.5 1.0
CA A:PRO132 4.1 19.3 1.0
O A:HOH319 4.2 28.7 1.0
O A:HOH276 4.3 19.6 1.0
OD2 A:ASP135 4.4 20.6 1.0
C A:TRP23 4.4 16.3 1.0
OH A:TYR138 4.4 14.7 1.0
CZ A:TYR138 4.5 13.2 1.0
N A:PRO132 4.6 19.4 1.0
O A:HOH369 4.6 30.0 1.0
CG A:TRP23 4.6 15.2 1.0
CD2 A:TRP23 4.6 13.0 1.0
CA A:TRP23 4.7 16.5 1.0
CD2 A:TYR138 4.7 13.4 1.0
C A:ALA131 4.8 19.5 1.0
O A:ALA131 4.8 19.6 1.0
O A:HOH373 4.8 27.9 1.0
C A:ARG130 4.9 20.3 1.0
CZ3 A:TRP23 5.0 16.4 1.0

Reference:

D.R.Davies, B.L.Staker, J.A.Abendroth, T.E.Edwards, R.Hartley, J.Leonard, H.Kim, A.L.Rychel, S.N.Hewitt, P.J.Myler, L.J.Stewart. An Ensemble of Structures of Burkholderia Pseudomallei 2,3-Bisphosphoglycerate-Dependent Phosphoglycerate Mutase. Acta Crystallogr.,Sect.F V. 67 1044 2011.
ISSN: ESSN 1744-3091
PubMed: 21904048
DOI: 10.1107/S1744309111030405
Page generated: Mon Oct 7 11:22:30 2024

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