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

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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: Mon Oct 7 08:51:43 2024

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