Potassium in PDB 4lng: Aspergillus Fumigatus Protein Farnesyltransferase Complex with Farnesyldiphosphate and Tipifarnib

Enzymatic activity of Aspergillus Fumigatus Protein Farnesyltransferase Complex with Farnesyldiphosphate and Tipifarnib

All present enzymatic activity of Aspergillus Fumigatus Protein Farnesyltransferase Complex with Farnesyldiphosphate and Tipifarnib:
2.5.1.58;

Protein crystallography data

The structure of Aspergillus Fumigatus Protein Farnesyltransferase Complex with Farnesyldiphosphate and Tipifarnib, PDB code: 4lng was solved by M.F.Mabanglo, M.A.Hast, L.S.Beese, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	30.24 / 1.91
*Space group*	P 1 2₁ 1
*Cell size a, b, c (Å), α, β, γ (°)*	63.537, 90.658, 83.163, 90.00, 111.09, 90.00
*R / R_free (%)*	15.5 / 18.4

Other elements in 4lng:

The structure of Aspergillus Fumigatus Protein Farnesyltransferase Complex with Farnesyldiphosphate and Tipifarnib also contains other interesting chemical elements:

Chlorine	(Cl)	2 atoms
Zinc	(Zn)	1 atom

Potassium Binding Sites:

The binding sites of Potassium atom in the Aspergillus Fumigatus Protein Farnesyltransferase Complex with Farnesyldiphosphate and Tipifarnib (pdb code 4lng). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Aspergillus Fumigatus Protein Farnesyltransferase Complex with Farnesyldiphosphate and Tipifarnib, PDB code: 4lng:

Potassium binding site 1 out of 1 in 4lng

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Potassium Binding Sites List in 4lng

Potassium binding site 1 out of 1 in the Aspergillus Fumigatus Protein Farnesyltransferase Complex with Farnesyldiphosphate and Tipifarnib

Mono view

Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Aspergillus Fumigatus Protein Farnesyltransferase Complex with Farnesyldiphosphate and Tipifarnib within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
B:K607 b:26.0 occ:1.00	O2	B:EDO605	2.9	32.9	1.0
	NH1	B:ARG252	3.2	21.3	1.0
	NE1	B:TRP153	3.3	12.1	1.0
	O	A:HOH740	3.3	47.0	1.0
	CB	B:ALA201	3.4	10.3	1.0
	C25	B:JAN602	3.8	19.9	0.9
	C2	B:EDO605	3.8	30.7	1.0
	CD1	B:TRP153	4.2	14.1	1.0
	CE2	B:TRP153	4.2	13.8	1.0
	OH	A:TYR109	4.2	43.8	1.0
	CE1	B:HIS199	4.3	14.7	1.0
	CL1	B:JAN602	4.4	24.6	0.9
	CD	B:ARG252	4.4	22.6	1.0
	C1	B:EDO605	4.4	30.8	1.0
	C14	B:FPP603	4.4	19.9	1.0
	CZ	B:ARG252	4.4	22.3	1.0
	CZ2	B:TRP153	4.5	13.3	1.0
	O	A:HOH741	4.6	53.6	1.0
	C26	B:JAN602	4.7	18.0	0.9
	CL2	B:JAN602	4.8	18.5	0.9
	C24	B:JAN602	4.9	15.9	0.9
	NE	B:ARG252	4.9	24.5	1.0
	NE2	B:HIS199	4.9	15.3	1.0
	CA	B:ALA201	5.0	13.5	1.0
	ND1	B:HIS199	5.0	13.9	1.0

Reference:

M.F.Mabanglo, M.A.Hast, N.B.Lubock, H.W.Hellinga, L.S.Beese. Crystal Structures of the Fungal Pathogen Aspergillus Fumigatus Protein Farnesyltransferase Complexed with Substrates and Inhibitors Reveal Features For Antifungal Drug Design. Protein Sci. V. 23 289 2014.
ISSN: ISSN 0961-8368
PubMed: 24347326
DOI: 10.1002/PRO.2411

Page generated: Mon Aug 12 11:29:00 2024

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