Manganese in PDB 1ad4: Dihydropteroate Synthetase Complexed with Oh-CH2-Pterin- Pyrophosphate From Staphylococcus Aureus

Enzymatic activity of Dihydropteroate Synthetase Complexed with Oh-CH2-Pterin- Pyrophosphate From Staphylococcus Aureus

All present enzymatic activity of Dihydropteroate Synthetase Complexed with Oh-CH2-Pterin- Pyrophosphate From Staphylococcus Aureus:
2.5.1.15;

Protein crystallography data

The structure of Dihydropteroate Synthetase Complexed with Oh-CH2-Pterin- Pyrophosphate From Staphylococcus Aureus, PDB code: 1ad4 was solved by C.Oefner, D.Kostrewa, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	13.00 / 2.40
*Space group*	P 1 2₁ 1
*Cell size a, b, c (Å), α, β, γ (°)*	65.748, 42.142, 99.040, 90.00, 106.06, 90.00
*R / R_free (%)*	17.6 / n/a

Other elements in 1ad4:

The structure of Dihydropteroate Synthetase Complexed with Oh-CH2-Pterin- Pyrophosphate From Staphylococcus Aureus also contains other interesting chemical elements:

Potassium

(K)

2 atoms

Manganese Binding Sites:

The binding sites of Manganese atom in the Dihydropteroate Synthetase Complexed with Oh-CH2-Pterin- Pyrophosphate From Staphylococcus Aureus (pdb code 1ad4). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 3 binding sites of Manganese where determined in the Dihydropteroate Synthetase Complexed with Oh-CH2-Pterin- Pyrophosphate From Staphylococcus Aureus, PDB code: 1ad4:
Jump to Manganese binding site number: 1; 2; 3;

Manganese binding site 1 out of 3 in 1ad4

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Manganese Binding Sites List in 1ad4

Manganese binding site 1 out of 3 in the Dihydropteroate Synthetase Complexed with Oh-CH2-Pterin- Pyrophosphate From Staphylococcus Aureus

Mono view

Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Dihydropteroate Synthetase Complexed with Oh-CH2-Pterin- Pyrophosphate From Staphylococcus Aureus within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Mn268 b:42.3 occ:1.00	O	B:HOH423	2.1	65.2	1.0
	O	A:HOH413	2.2	43.9	1.0
	NE2	A:HIS264	2.4	36.7	1.0
	O	B:HOH422	2.4	67.2	1.0
	CD2	A:HIS264	3.0	28.7	1.0
	CE1	A:HIS264	3.5	38.6	1.0
	OD2	B:ASP187	4.0	26.8	1.0
	CG	A:HIS264	4.2	39.1	1.0
	OD1	B:ASP187	4.3	22.7	1.0
	ND1	A:HIS264	4.4	40.2	1.0
	OE2	B:GLU188	4.5	17.4	1.0
	CG	B:ASP187	4.5	23.2	1.0

Manganese binding site 2 out of 3 in 1ad4

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Manganese Binding Sites List in 1ad4

Manganese binding site 2 out of 3 in the Dihydropteroate Synthetase Complexed with Oh-CH2-Pterin- Pyrophosphate From Staphylococcus Aureus

Mono view

Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Dihydropteroate Synthetase Complexed with Oh-CH2-Pterin- Pyrophosphate From Staphylococcus Aureus within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Mn269 b:37.7 occ:1.00	O6P	A:HH2271	2.0	16.8	1.0
	O	A:HOH407	2.3	34.6	1.0
	O	A:HOH362	2.3	29.3	1.0
	OD1	A:ASN11	2.4	34.0	1.0
	P2	A:HH2271	3.5	18.1	1.0
	O2P	A:HH2271	3.6	14.8	1.0
	CG	A:ASN11	3.6	28.4	1.0
	NH2	A:ARG239	4.1	9.9	1.0
	O3P	A:HH2271	4.1	14.1	1.0
	O	A:HOH406	4.1	23.5	1.0
	O	A:VAL49	4.2	29.8	1.0
	O	A:HOH326	4.2	18.1	1.0
	O4	A:HH2271	4.2	11.7	1.0
	P1	A:HH2271	4.2	15.1	1.0
	O5P	A:HH2271	4.3	1.1	1.0
	ND2	A:ASN11	4.3	26.4	1.0
	C3	A:HH2271	4.4	14.6	1.0
	O4P	A:HH2271	4.5	11.1	1.0
	OD2	A:ASP84	4.7	22.0	1.0
	CB	A:ASN11	4.8	21.2	1.0
	O	A:GLY47	4.8	23.4	1.0
	C	A:GLY47	4.9	19.6	1.0

Manganese binding site 3 out of 3 in 1ad4

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Manganese Binding Sites List in 1ad4

Manganese binding site 3 out of 3 in the Dihydropteroate Synthetase Complexed with Oh-CH2-Pterin- Pyrophosphate From Staphylococcus Aureus

Mono view

Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Dihydropteroate Synthetase Complexed with Oh-CH2-Pterin- Pyrophosphate From Staphylococcus Aureus within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
B:Mn1 b:27.9 occ:1.00	O	A:HOH372	2.1	34.5	1.0
	NE2	B:HIS264	2.2	20.4	1.0
	O	A:HOH357	2.3	16.0	1.0
	O	B:HOH416	2.3	29.1	1.0
	O	B:HOH417	2.5	37.8	1.0
	CD2	B:HIS264	3.0	11.2	1.0
	CE1	B:HIS264	3.3	15.3	1.0
	OD2	A:ASP187	4.1	19.7	1.0
	CG	B:HIS264	4.2	13.6	1.0
	OD1	A:ASP187	4.2	21.9	1.0
	OE2	A:GLU188	4.2	6.3	1.0
	ND1	B:HIS264	4.2	11.5	1.0
	CG	A:ASP187	4.6	16.3	1.0
	O	A:ALA184	4.8	10.3	1.0
	O	A:HOH288	4.9	12.9	1.0

Reference:

I.C.Hampele, A.D'arcy, G.E.Dale, D.Kostrewa, J.Nielsen, C.Oefner, M.G.Page, H.J.Schonfeld, D.Stuber, R.L.Then. Structure and Function of the Dihydropteroate Synthase From Staphylococcus Aureus. J.Mol.Biol. V. 268 21 1997.
ISSN: ISSN 0022-2836
PubMed: 9149138
DOI: 10.1006/JMBI.1997.0944

Page generated: Sat Oct 5 09:43:41 2024

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