Magnesium in PDB 2fwn: Phosphorylation of An Active Site Serine in A Thdp- Dependent Enzyme By Phosphonate Inactivation

Enzymatic activity of Phosphorylation of An Active Site Serine in A Thdp- Dependent Enzyme By Phosphonate Inactivation

All present enzymatic activity of Phosphorylation of An Active Site Serine in A Thdp- Dependent Enzyme By Phosphonate Inactivation:
4.1.1.7;

Protein crystallography data

The structure of Phosphorylation of An Active Site Serine in A Thdp- Dependent Enzyme By Phosphonate Inactivation, PDB code: 2fwn was solved by A.K.Bera, M.S.Hasson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	50.00 / 1.40
*Space group*	I 2 2 2
*Cell size a, b, c (Å), α, β, γ (°)*	81.165, 95.039, 137.363, 90.00, 90.00, 90.00
*R / R_free (%)*	10.8 / n/a

Other elements in 2fwn:

The structure of Phosphorylation of An Active Site Serine in A Thdp- Dependent Enzyme By Phosphonate Inactivation also contains other interesting chemical elements:

Calcium

(Ca)

3 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Phosphorylation of An Active Site Serine in A Thdp- Dependent Enzyme By Phosphonate Inactivation (pdb code 2fwn). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Phosphorylation of An Active Site Serine in A Thdp- Dependent Enzyme By Phosphonate Inactivation, PDB code: 2fwn:

Magnesium binding site 1 out of 1 in 2fwn

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Magnesium Binding Sites List in 2fwn

Magnesium binding site 1 out of 1 in the Phosphorylation of An Active Site Serine in A Thdp- Dependent Enzyme By Phosphonate Inactivation

Mono view

Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Phosphorylation of An Active Site Serine in A Thdp- Dependent Enzyme By Phosphonate Inactivation within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Mg531 b:6.5 occ:0.50	O	A:LEU118	2.5	6.0	1.0
	O	A:ARG120	2.5	7.3	1.0
	O	A:ASN117	2.7	6.5	1.0
	O	A:HOH1214	3.2	36.7	0.5
	C	A:LEU118	3.3	6.4	1.0
	C	A:ARG120	3.6	6.9	1.0
	CA	A:LEU118	3.8	5.9	1.0
	C	A:ASN117	3.8	6.6	1.0
	N	A:ARG120	3.8	6.6	1.0
	CA	A:ARG120	4.2	7.0	1.0
	N	A:PRO119	4.2	6.3	1.0
	N	A:LEU118	4.3	5.6	1.0
	C	A:PRO119	4.3	6.3	1.0
	CE	A:MET79	4.3	15.0	0.4
	CB	A:ARG120	4.5	7.2	1.0
	CA	A:PRO119	4.6	6.8	1.0
	N	A:PRO121	4.7	6.2	1.0
	CD	A:PRO121	4.9	7.4	1.0
	O	A:PRO119	5.0	7.9	1.0

Reference:

A.K.Bera, L.S.Polovnikova, J.Roestamadji, T.S.Widlanski, G.L.Kenyon, M.J.Mcleish, M.S.Hasson. Mechanism-Based Inactivation of Benzoylformate Decarboxylase, A Thiamin Diphosphate-Dependent Enzyme J.Am.Chem.Soc. V. 129 4120 2007.
ISSN: ISSN 0002-7863
PubMed: 17367138
DOI: 10.1021/JA068636Z

Page generated: Tue Aug 13 23:19:28 2024

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