Sodium in PDB 4a21: Structure of Mycobacterium Tuberculosis Fructose 1,6- Bisphosphate Aldolase Bound to Sulfate

All present enzymatic activity of Structure of Mycobacterium Tuberculosis Fructose 1,6- Bisphosphate Aldolase Bound to Sulfate:
4.1.2.13;

The structure of Structure of Mycobacterium Tuberculosis Fructose 1,6- Bisphosphate Aldolase Bound to Sulfate, PDB code: 4a21 was solved by M.Coincon, M.De La Paz Santangelo, P.M.Gest, M.E.Guerin, H.Pham, G.Ryan, S.E.Puckett, J.S.Spencer, M.Gonzalez-Juarrero, R.Daher, A.J.Lenaerts, D.Schnappinger, M.Therisod, S.Ehrt, M.Jackson, J.Sygusch, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.873 / 2.35
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	336.945, 43.234, 103.020, 90.00, 99.57, 90.00
R / Rfree (%)	21.13 / 26.1

The binding sites of Sodium atom in the Structure of Mycobacterium Tuberculosis Fructose 1,6- Bisphosphate Aldolase Bound to Sulfate (pdb code 4a21). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Structure of Mycobacterium Tuberculosis Fructose 1,6- Bisphosphate Aldolase Bound to Sulfate, PDB code: 4a21:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in the Structure of Mycobacterium Tuberculosis Fructose 1,6- Bisphosphate Aldolase Bound to Sulfate


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Structure of Mycobacterium Tuberculosis Fructose 1,6- Bisphosphate Aldolase Bound to Sulfate within 5.0Å range: probe atom residue distance (Å) B Occ A:Na1346 b:47.2 occ:1.00 HE2 A:HIS93 2.7 31.1 1.0 HD22 A:ASN274 2.8 47.8 1.0 OD1 A:ASP95 3.0 58.1 1.0 HZ2 A:LYS272 3.0 30.9 1.0 HA A:ASP95 3.2 34.6 1.0 HZ3 A:LYS272 3.3 30.9 1.0 OE1 A:GLU159 3.3 32.1 1.0 HE22 A:GLN51 3.3 40.0 1.0 HD2 A:HIS93 3.4 26.9 1.0 OE2 A:GLU159 3.4 39.3 1.0 NE2 A:HIS93 3.4 25.9 1.0 OE1 A:GLN51 3.4 34.5 1.0 ND2 A:ASN274 3.4 39.9 1.0 NZ A:LYS272 3.6 25.7 1.0 CD A:GLU159 3.6 37.8 1.0 HB2 A:MET129 3.6 24.7 1.0 SD A:MET129 3.6 44.0 1.0 HE1 A:HIS252 3.7 57.4 1.0 H A:HIS96 3.7 61.0 1.0 CG A:ASP95 3.7 53.2 1.0 CD2 A:HIS93 3.7 22.4 1.0 HE2 A:HIS252 3.8 51.7 1.0 NE2 A:GLN51 3.9 33.3 1.0 HD21 A:ASN274 3.9 47.8 1.0 CD A:GLN51 3.9 32.4 1.0 OD1 A:ASN274 4.0 35.7 1.0 CE1 A:HIS252 4.0 47.8 1.0 CG A:ASN274 4.0 36.5 1.0 HZ1 A:LYS272 4.0 30.9 1.0 NE2 A:HIS252 4.1 43.1 1.0 CA A:ASP95 4.1 28.9 1.0 HB2 A:ASP95 4.1 45.1 1.0 CB A:ASP95 4.2 37.6 1.0 CB A:MET129 4.3 20.6 1.0 HB3 A:MET129 4.3 24.7 1.0 N A:HIS96 4.4 50.9 1.0 HG12 A:VAL250 4.4 33.3 1.0 O A:HOH2085 4.4 41.0 1.0 OD2 A:ASP95 4.5 42.5 1.0 CG A:MET129 4.5 28.5 1.0 O A:THR94 4.5 26.2 1.0 HE3 A:LYS272 4.5 27.5 1.0 HE21 A:GLN51 4.6 40.0 1.0 CE1 A:HIS93 4.6 24.1 1.0 HD2 A:HIS96 4.6 68.2 1.0 CE A:LYS272 4.7 22.9 1.0 C A:ASP95 4.8 38.9 1.0 CG A:GLU159 4.9 25.8 1.0 HG3 A:MET129 4.9 34.2 1.0 HG2 A:GLU159 4.9 30.9 1.0 CD2 A:HIS96 4.9 56.9 1.0 ND1 A:HIS252 5.0 53.8 1.0

Sodium binding site 2 out of 2 in the Structure of Mycobacterium Tuberculosis Fructose 1,6- Bisphosphate Aldolase Bound to Sulfate


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of Structure of Mycobacterium Tuberculosis Fructose 1,6- Bisphosphate Aldolase Bound to Sulfate within 5.0Å range: probe atom residue distance (Å) B Occ A:Na1347 b:43.1 occ:1.00 HB2 A:CYS97 2.6 25.5 1.0 H A:MET129 2.8 21.1 1.0 OG1 A:THR94 3.0 22.4 1.0 O A:MET129 3.1 21.4 1.0 HB3 A:MET129 3.1 24.7 1.0 HG1 A:THR94 3.1 26.8 1.0 HB A:THR94 3.1 27.0 1.0 O A:ASP95 3.2 41.9 1.0 C A:THR94 3.3 25.0 1.0 N A:ASP95 3.3 24.2 1.0 O A:THR94 3.3 26.2 1.0 HB3 A:CYS97 3.3 25.5 1.0 C A:ASP95 3.4 38.9 1.0 CB A:CYS97 3.4 21.2 1.0 H A:ASP95 3.5 29.0 1.0 CB A:THR94 3.5 22.5 1.0 HG23 A:VAL106 3.5 34.7 1.0 N A:MET129 3.5 17.6 1.0 HE2 A:TYR105 3.6 35.0 1.0 HG21 A:VAL106 3.7 34.7 1.0 CA A:ASP95 3.8 28.9 1.0 H A:CYS97 3.8 32.7 1.0 N A:CYS97 3.8 27.2 1.0 C A:MET129 3.8 20.2 1.0 CB A:MET129 3.9 20.6 1.0 CA A:MET129 3.9 19.8 1.0 CG2 A:VAL106 3.9 28.9 1.0 HD2 A:TYR105 3.9 34.1 1.0 HA A:ASP95 3.9 34.6 1.0 N A:HIS96 3.9 50.9 1.0 HG22 A:VAL106 4.0 34.7 1.0 CA A:THR94 4.0 24.8 1.0 C A:HIS96 4.1 33.3 1.0 CE2 A:TYR105 4.1 29.1 1.0 CA A:CYS97 4.2 28.8 1.0 CD2 A:TYR105 4.3 28.4 1.0 H A:HIS96 4.4 61.0 1.0 HB2 A:MET129 4.4 24.7 1.0 HA A:HIS128 4.5 23.3 1.0 CA A:HIS96 4.5 41.5 1.0 O A:HIS96 4.6 37.3 1.0 HA A:CYS97 4.6 34.6 1.0 HA A:THR94 4.6 29.8 1.0 HG2 A:MET129 4.6 34.2 1.0 C A:HIS128 4.7 19.4 1.0 SG A:CYS97 4.7 35.5 1.0 HB3 A:HIS128 4.8 21.6 1.0 HD1 A:HIS128 4.8 30.0 1.0 HA A:HIS96 4.8 49.8 1.0 HA A:MET129 4.9 23.8 1.0 CG2 A:THR94 4.9 23.1 1.0 CG A:MET129 4.9 28.5 1.0 HG23 A:THR54 4.9 34.0 1.0 H A:THR94 4.9 24.4 1.0 HG21 A:THR54 4.9 34.0 1.0 HG22 A:THR94 4.9 27.8 1.0

M.De La Paz Santangelo, P.M.Gest, M.E.Guerin, M.Coincon, H.Pham, G.Ryan, S.E.Puckett, J.S.Spencer, M.Gonzalez-Juarrero, R.Daher, A.J.Lenaerts, D.Schnappinger, M.Therisod, S.Ehrt, J.Sygusch, M.Jackson. Glycolytic and Non-Glycolytic Functions of the Fructose- 1,6-Bisphosphate Aldolase of Mycobacterium Tuberculosis, An Essential Enzyme Produced By Replicating and Non-Replicating Bacilli J.Biol.Chem. V. 286 40219 2011.
ISSN: ISSN 0021-9258
PubMed: 21949126
DOI: 10.1074/JBC.M111.259440