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Sodium in PDB 3aez: Pantothenate Kinase From Mycobacterium Tuberculosis (Mtpank) in Complex with Gdp and Phosphopantothenate

Enzymatic activity of Pantothenate Kinase From Mycobacterium Tuberculosis (Mtpank) in Complex with Gdp and Phosphopantothenate

All present enzymatic activity of Pantothenate Kinase From Mycobacterium Tuberculosis (Mtpank) in Complex with Gdp and Phosphopantothenate:
2.7.1.33;

Protein crystallography data

The structure of Pantothenate Kinase From Mycobacterium Tuberculosis (Mtpank) in Complex with Gdp and Phosphopantothenate, PDB code: 3aez was solved by B.Chetnani, P.Kumar, A.Surolia, M.Vijayan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 34.06 / 2.20
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 103.640, 103.640, 90.410, 90.00, 90.00, 120.00
R / Rfree (%) 20.3 / 24.3

Sodium Binding Sites:

The binding sites of Sodium atom in the Pantothenate Kinase From Mycobacterium Tuberculosis (Mtpank) in Complex with Gdp and Phosphopantothenate (pdb code 3aez). 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 Pantothenate Kinase From Mycobacterium Tuberculosis (Mtpank) in Complex with Gdp and Phosphopantothenate, PDB code: 3aez:

Sodium binding site 1 out of 1 in 3aez

Go back to Sodium Binding Sites List in 3aez
Sodium binding site 1 out of 1 in the Pantothenate Kinase From Mycobacterium Tuberculosis (Mtpank) in Complex with Gdp and Phosphopantothenate


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Pantothenate Kinase From Mycobacterium Tuberculosis (Mtpank) in Complex with Gdp and Phosphopantothenate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na328

b:51.4
occ:1.00
 O A:ALA100 2.6 28.0 1.0
OE2 A:GLU42 2.7 51.9 1.0
O A:HOH509 2.8 36.9 1.0
O A:HOH402 3.2 35.7 1.0
C A:ALA100 3.4 24.8 1.0
N A:GLY102 3.5 26.6 1.0
CD A:GLU42 3.7 51.0 1.0
C A:VAL101 3.8 27.1 1.0
NE2 A:HIS302 3.8 34.9 1.0
CD2 A:HIS302 3.9 34.2 1.0
CG A:GLU42 3.9 43.3 1.0
CA A:GLY102 3.9 26.0 1.0
N A:VAL101 4.1 25.4 1.0
CE3 A:TRP234 4.2 23.7 1.0
CA A:ALA100 4.2 26.1 1.0
O A:VAL101 4.3 29.5 1.0
CA A:VAL101 4.3 23.9 1.0
O1B A:GDP313 4.5 24.1 1.0
CB A:TRP234 4.7 27.6 1.0
O A:HOH338 4.7 32.0 1.0
O A:LEU40 4.8 32.6 1.0
OE1 A:GLU42 4.8 56.5 1.0
CD2 A:TRP234 4.8 24.7 1.0
O A:HOH367 4.9 29.7 1.0
CZ3 A:TRP234 4.9 30.8 1.0
CB A:ALA100 4.9 22.7 1.0
NH1 A:ARG238 4.9 22.4 1.0
C A:GLY41 5.0 36.7 1.0

Reference:

B.Chetnani, P.Kumar, A.Surolia, M.Vijayan. M. Tuberculosis Pantothenate Kinase: Dual Substrate Specificity and Unusual Changes in Ligand Locations J.Mol.Biol. V. 400 171 2010.
ISSN: ISSN 0022-2836
PubMed: 20451532
DOI: 10.1016/J.JMB.2010.04.064
Page generated: Mon Oct 7 05:46:26 2024

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