Magnesium in PDB 4em4: Crystal Structure of Staphylococcus Aureus Bound with the Covalent Inhibitor Pethyl-Vs-Coa

Enzymatic activity of Crystal Structure of Staphylococcus Aureus Bound with the Covalent Inhibitor Pethyl-Vs-Coa

All present enzymatic activity of Crystal Structure of Staphylococcus Aureus Bound with the Covalent Inhibitor Pethyl-Vs-Coa:
1.8.1.14;

Protein crystallography data

The structure of Crystal Structure of Staphylococcus Aureus Bound with the Covalent Inhibitor Pethyl-Vs-Coa, PDB code: 4em4 was solved by B.D.Wallace, J.S.Edwards, A.Claiborne, M.R.Redinbo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	32.46 / 1.82
*Space group*	P 1 2₁ 1
*Cell size a, b, c (Å), α, β, γ (°)*	76.144, 64.909, 94.442, 90.00, 104.62, 90.00
*R / R_free (%)*	15.4 / 20.2

Other elements in 4em4:

The structure of Crystal Structure of Staphylococcus Aureus Bound with the Covalent Inhibitor Pethyl-Vs-Coa also contains other interesting chemical elements:

Chlorine

(Cl)

7 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Staphylococcus Aureus Bound with the Covalent Inhibitor Pethyl-Vs-Coa (pdb code 4em4). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Crystal Structure of Staphylococcus Aureus Bound with the Covalent Inhibitor Pethyl-Vs-Coa, PDB code: 4em4:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in 4em4

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Magnesium Binding Sites List in 4em4

Magnesium binding site 1 out of 3 in the Crystal Structure of Staphylococcus Aureus Bound with the Covalent Inhibitor Pethyl-Vs-Coa

Mono view

Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Staphylococcus Aureus Bound with the Covalent Inhibitor Pethyl-Vs-Coa within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Mg502 b:37.6 occ:1.00	O	A:HOH1149	1.7	40.2	1.0
	O	A:HOH601	1.8	31.7	1.0
	O	A:HOH604	1.8	28.7	1.0
	O	A:HOH602	2.0	35.6	1.0
	O	A:HOH603	2.0	32.4	1.0
	O	A:HOH605	2.4	27.7	1.0
	O	A:HOH911	3.2	49.2	1.0
	O	A:HOH969	3.6	32.8	1.0
	OD1	A:ASN85	3.9	26.2	1.0
	O	A:HOH770	4.0	37.4	1.0
	O	A:HOH912	4.3	32.5	1.0
	O	A:ILE84	4.4	23.1	1.0
	O	A:HOH1157	4.4	25.3	1.0
	CA	A:ASN85	4.5	23.2	1.0
	O	A:HOH1017	4.5	38.1	1.0
	OG	A:SER248	4.6	22.6	1.0
	O	A:SER248	4.7	22.3	1.0
	CB	A:ASN85	4.8	22.1	1.0
	CG	A:ASN85	4.8	19.9	1.0

Magnesium binding site 2 out of 3 in 4em4

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Magnesium Binding Sites List in 4em4

Magnesium binding site 2 out of 3 in the Crystal Structure of Staphylococcus Aureus Bound with the Covalent Inhibitor Pethyl-Vs-Coa

Mono view

Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Staphylococcus Aureus Bound with the Covalent Inhibitor Pethyl-Vs-Coa within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Mg503 b:71.7 occ:1.00	O	A:HOH1082	1.8	50.7	1.0
	O	A:HOH821	1.9	51.2	1.0
	O	A:HOH695	2.0	44.6	1.0
	OE2	A:GLU54	3.7	70.5	1.0
	O	A:HOH807	3.7	45.9	1.0
	OE1	A:GLU51	3.8	43.4	1.0
	NZ	A:LYS144	4.0	48.3	1.0
	CG	A:GLU51	4.4	35.9	1.0
	CD	A:GLU51	4.4	42.5	1.0
	OD2	A:ASP140	4.5	34.4	1.0
	OD1	A:ASP140	4.6	29.5	1.0
	CE	A:LYS144	4.7	41.2	1.0
	CD	A:GLU54	4.9	77.5	1.0
	CG	A:ASP140	4.9	41.0	1.0

Magnesium binding site 3 out of 3 in 4em4

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Magnesium Binding Sites List in 4em4

Magnesium binding site 3 out of 3 in the Crystal Structure of Staphylococcus Aureus Bound with the Covalent Inhibitor Pethyl-Vs-Coa

Mono view

Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of Staphylococcus Aureus Bound with the Covalent Inhibitor Pethyl-Vs-Coa within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
B:Mg502 b:52.9 occ:1.00	O	B:HOH1103	1.9	46.4	1.0
	O	B:HOH910	1.9	46.3	1.0
	O	B:HOH1104	1.9	50.5	1.0
	O	B:HOH1049	1.9	43.0	1.0
	O	B:HOH1102	2.2	55.5	1.0
	O	B:HOH647	2.2	35.8	1.0
	OD2	B:ASP140	4.2	40.3	1.0
	O	B:HOH809	4.2	41.9	1.0
	NZ	B:LYS144	4.3	56.4	1.0
	OE1	B:GLU51	4.3	39.2	1.0
	OE2	B:GLU54	4.3	58.1	1.0
	OD1	B:ASP140	4.4	36.0	1.0
	O	B:HOH839	4.5	39.3	1.0
	CG	B:ASP140	4.6	38.0	1.0
	CG	B:GLU51	4.8	31.4	1.0
	CE	B:LYS144	4.8	41.5	1.0
	CD	B:GLU51	5.0	43.1	1.0

Reference:

B.D.Wallace, J.S.Edwards, J.R.Wallen, W.J.Moolman, R.Van Der Westhuyzen, E.Strauss, M.R.Redinbo, A.Claiborne. Turnover-Dependent Covalent Inactivation of Staphylococcus Aureus Coenzyme A-Disulfide Reductase By Coenzyme A-Mimetics: Mechanistic and Structural Insights. Biochemistry V. 51 7699 2012.
ISSN: ISSN 0006-2960
PubMed: 22954034
DOI: 10.1021/BI301026C

Page generated: Fri Aug 16 14:32:00 2024

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