Sodium in PDB 3ekz: Structural Characterization of Tetrameric Mycobacterium Tuberculosis Fructose 1,6-Bisphosphate Aldolase - Substrate Binding and Catalysis Mechanism of A Class Iia Bacterial Aldolase

Enzymatic activity of Structural Characterization of Tetrameric Mycobacterium Tuberculosis Fructose 1,6-Bisphosphate Aldolase - Substrate Binding and Catalysis Mechanism of A Class Iia Bacterial Aldolase

All present enzymatic activity of Structural Characterization of Tetrameric Mycobacterium Tuberculosis Fructose 1,6-Bisphosphate Aldolase - Substrate Binding and Catalysis Mechanism of A Class Iia Bacterial Aldolase:
4.1.2.13;

Protein crystallography data

The structure of Structural Characterization of Tetrameric Mycobacterium Tuberculosis Fructose 1,6-Bisphosphate Aldolase - Substrate Binding and Catalysis Mechanism of A Class Iia Bacterial Aldolase, PDB code: 3ekz was solved by S.Pegan, K.Rukseree, S.G.Franzblau, A.D.Mesecar, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	25.90 / 2.07
*Space group*	I 2 2 2
*Cell size a, b, c (Å), α, β, γ (°)*	61.220, 120.486, 164.327, 90.00, 90.00, 90.00
*R / R_free (%)*	15.8 / 18

Other elements in 3ekz:

Zinc

(Zn)

2 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Structural Characterization of Tetrameric Mycobacterium Tuberculosis Fructose 1,6-Bisphosphate Aldolase - Substrate Binding and Catalysis Mechanism of A Class Iia Bacterial Aldolase (pdb code 3ekz). 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 Structural Characterization of Tetrameric Mycobacterium Tuberculosis Fructose 1,6-Bisphosphate Aldolase - Substrate Binding and Catalysis Mechanism of A Class Iia Bacterial Aldolase, PDB code: 3ekz:

Sodium binding site 1 out of 1 in 3ekz

Go back to

Sodium Binding Sites List in 3ekz

Sodium binding site 1 out of 1 in the Structural Characterization of Tetrameric Mycobacterium Tuberculosis Fructose 1,6-Bisphosphate Aldolase - Substrate Binding and Catalysis Mechanism of A Class Iia Bacterial Aldolase

Mono view

Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Structural Characterization of Tetrameric Mycobacterium Tuberculosis Fructose 1,6-Bisphosphate Aldolase - Substrate Binding and Catalysis Mechanism of A Class Iia Bacterial Aldolase within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Na353 b:17.6 occ:1.00	O1P	A:13P350	2.2	12.8	0.3
	O	A:GLY213	2.4	11.7	1.0
	O	A:SER255	2.4	18.1	1.0
	O	A:HOH631	2.5	28.9	1.0
	O1P	A:13P351	2.6	18.9	0.7
	O	A:GLY253	2.6	16.4	1.0
	O	A:VAL211	2.7	15.5	1.0
	C	A:GLY253	3.2	16.7	1.0
	C	A:SER255	3.5	18.2	1.0
	N	A:GLY213	3.5	14.6	1.0
	C	A:GLY213	3.5	13.0	1.0
	N	A:SER255	3.7	18.1	1.0
	CA	A:GLY253	3.7	17.2	1.0
	P	A:13P350	3.7	14.3	0.3
	C	A:VAL211	3.9	15.4	1.0
	CA	A:SER255	3.9	18.5	1.0
	O	A:HOH620	4.0	21.7	1.0
	P	A:13P351	4.0	18.9	0.7
	CB	A:SER255	4.1	17.8	1.0
	C	A:HIS212	4.1	15.8	1.0
	N	A:GLY254	4.2	16.7	1.0
	CA	A:GLY213	4.2	13.5	1.0
	C	A:GLY254	4.2	18.9	1.0
	CA	A:HIS212	4.3	16.3	1.0
	O3P	A:13P351	4.3	17.0	0.7
	O3P	A:13P350	4.4	15.2	0.3
	O1	A:13P350	4.4	15.1	0.3
	O	A:HOH421	4.5	21.9	1.0
	O	A:HOH430	4.5	18.4	1.0
	N	A:HIS212	4.6	15.2	1.0
	O2P	A:13P350	4.6	12.2	0.3
	N	A:VAL214	4.6	13.5	1.0
	N	A:GLY256	4.6	18.1	1.0
	CA	A:GLY254	4.7	17.7	1.0
	O	A:GLY254	4.7	18.1	1.0
	O1	A:13P351	4.8	21.1	0.7
	CA	A:VAL214	4.8	14.4	1.0

Reference:

S.D.Pegan, K.Rukseree, S.G.Franzblau, A.D.Mesecar. Structural Basis For Catalysis of A Tetrameric Class Iia Fructose 1,6-Bisphosphate Aldolase From Mycobacterium Tuberculosis J.Mol.Biol. V. 386 1038 2009.
ISSN: ISSN 0022-2836
PubMed: 19167403
DOI: 10.1016/J.JMB.2009.01.003

Page generated: Tue Dec 15 06:09:51 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3

	© Copyright 2008-2020 by atomistry.com
Home \| Site Map \| Copyright \| Contact us \| Privacy