Sodium in PDB 5coq: The Effect of Valine to Alanine Mutation on Inha Enzyme Crystallization Pattern and Substrate Binding Loop Conformation and Flexibility

Enzymatic activity of The Effect of Valine to Alanine Mutation on Inha Enzyme Crystallization Pattern and Substrate Binding Loop Conformation and Flexibility

All present enzymatic activity of The Effect of Valine to Alanine Mutation on Inha Enzyme Crystallization Pattern and Substrate Binding Loop Conformation and Flexibility:
1.3.1.9;

Protein crystallography data

The structure of The Effect of Valine to Alanine Mutation on Inha Enzyme Crystallization Pattern and Substrate Binding Loop Conformation and Flexibility, PDB code: 5coq was solved by H.-J.Li, C.-T.Lai, N.Liu, W.Yu, S.Shah, G.R.Bommineni, V.Perrone, M.Garcia-Diaz, P.J.Tonge, C.Simmerling, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	46.07 / 2.30
*Space group*	C 1 2 1
*Cell size a, b, c (Å), α, β, γ (°)*	126.095, 91.903, 102.846, 90.00, 106.45, 90.00
*R / R_free (%)*	16.1 / 21.2

Sodium Binding Sites:

The binding sites of Sodium atom in the The Effect of Valine to Alanine Mutation on Inha Enzyme Crystallization Pattern and Substrate Binding Loop Conformation and Flexibility (pdb code 5coq). 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 The Effect of Valine to Alanine Mutation on Inha Enzyme Crystallization Pattern and Substrate Binding Loop Conformation and Flexibility, PDB code: 5coq:

Sodium binding site 1 out of 1 in 5coq

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Sodium Binding Sites List in 5coq

Sodium binding site 1 out of 1 in the The Effect of Valine to Alanine Mutation on Inha Enzyme Crystallization Pattern and Substrate Binding Loop Conformation and Flexibility

Mono view

Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of The Effect of Valine to Alanine Mutation on Inha Enzyme Crystallization Pattern and Substrate Binding Loop Conformation and Flexibility within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
C:Na303 b:29.5 occ:1.00	O	C:ALA226	2.4	35.5	1.0
	O	C:HOH472	2.5	50.6	1.0
	O	C:ASP223	2.7	43.3	1.0
	O	C:HOH479	2.7	51.3	1.0
	O	C:GLN224	2.8	38.1	1.0
	C	C:GLN224	3.5	41.0	1.0
	C	C:ALA226	3.5	35.0	1.0
	O	C:HOH412	3.7	53.5	1.0
	C	C:ASP223	3.8	45.7	1.0
	CA	C:GLN224	3.8	46.5	1.0
	N	C:GLY229	4.2	35.3	1.0
	N	C:GLN224	4.2	46.9	1.0
	N	C:ALA226	4.3	39.4	1.0
	CA	C:GLY229	4.4	35.8	1.0
	N	C:PRO227	4.4	32.9	1.0
	CA	C:PRO227	4.4	32.6	1.0
	CA	C:ALA226	4.4	32.6	1.0
	C	C:PRO227	4.4	37.6	1.0
	N	C:ARG225	4.5	41.2	1.0
	O	C:PRO227	4.5	38.4	1.0
	C	C:ARG225	4.6	38.5	1.0
	O	C:HOH478	4.8	52.0	1.0
	CB	C:ALA226	4.9	34.5	1.0
	N	C:ILE228	5.0	33.4	1.0
	O	C:ARG225	5.0	37.5	1.0

Reference:

C.T.Lai, H.J.Li, W.Yu, S.Shah, G.R.Bommineni, V.Perrone, M.Garcia-Diaz, P.J.Tonge, C.Simmerling. Rational Modulation of the Induced-Fit Conformational Change For Slow-Onset Inhibition in Mycobacterium Tuberculosis Inha. Biochemistry V. 54 4683 2015.
ISSN: ISSN 0006-2960
PubMed: 26147157
DOI: 10.1021/ACS.BIOCHEM.5B00284

Page generated: Mon Oct 7 20:24:35 2024

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