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Zinc 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 / Rfree (%) 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:

Potassium (K) 1 atom
Chlorine (Cl) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc 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 Zinc atom.
In total only one binding site of Zinc was determined in the Aspergillus Fumigatus Protein Farnesyltransferase Complex with Farnesyldiphosphate and Tipifarnib, PDB code: 4lng:

Zinc binding site 1 out of 1 in 4lng

Go back to Zinc Binding Sites List in 4lng
Zinc 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 Zinc with other atoms in the Zn 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:Zn601

b:13.2
occ:1.00
 NE2 B:HIS433 2.1 12.2 1.0
OD2 B:ASP365 2.1 14.2 1.0
N2 B:JAN602 2.2 12.1 0.9
SG B:CYS367 2.3 11.4 1.0
OD1 B:ASP365 2.5 10.3 1.0
CG B:ASP365 2.6 12.2 1.0
CD2 B:HIS433 2.9 12.5 1.0
C2 B:JAN602 3.1 12.2 0.9
C3 B:JAN602 3.1 11.3 0.9
CE1 B:HIS433 3.2 11.9 1.0
CB B:CYS367 3.3 10.5 1.0
CE2 B:TYR432 3.7 9.1 1.0
CB B:ASP365 4.1 10.2 1.0
CG B:HIS433 4.1 11.5 1.0
N B:CYS367 4.2 11.0 1.0
ND1 B:HIS433 4.2 10.9 1.0
N1 B:JAN602 4.2 12.9 0.9
OH B:TYR432 4.3 10.1 1.0
C4 B:JAN602 4.3 11.0 0.9
CA B:CYS367 4.3 11.2 1.0
CG B:ASP423 4.4 16.4 1.0
O B:HOH1011 4.5 11.8 1.0
OD2 B:ASP423 4.5 19.9 1.0
CZ B:TYR432 4.5 10.3 1.0
O B:HOH830 4.6 30.3 1.0
CB B:ASP423 4.6 14.7 1.0
CD2 B:TYR432 4.7 9.6 1.0
OD1 B:ASP423 4.8 15.7 1.0
CA B:ASP423 4.9 10.6 1.0
CZ B:TYR368 5.0 11.6 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: Sun Oct 27 02:02:45 2024

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