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

Go back to

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

Go back to

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

Go back to

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

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW

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