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Zinc in PDB 4mbg: Crystal Structure of Aspergillus Fumigatus Protein Farnesyltransferase Binary Complex with Farnesyldiphosphate

Enzymatic activity of Crystal Structure of Aspergillus Fumigatus Protein Farnesyltransferase Binary Complex with Farnesyldiphosphate

All present enzymatic activity of Crystal Structure of Aspergillus Fumigatus Protein Farnesyltransferase Binary Complex with Farnesyldiphosphate:
2.5.1.58;

Protein crystallography data

The structure of Crystal Structure of Aspergillus Fumigatus Protein Farnesyltransferase Binary Complex with Farnesyldiphosphate, PDB code: 4mbg 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) 23.96 / 1.74
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 63.252, 90.793, 83.138, 90.00, 110.87, 90.00
R / Rfree (%) 12.2 / 16.4

Other elements in 4mbg:

The structure of Crystal Structure of Aspergillus Fumigatus Protein Farnesyltransferase Binary Complex with Farnesyldiphosphate also contains other interesting chemical elements:

Potassium (K) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Aspergillus Fumigatus Protein Farnesyltransferase Binary Complex with Farnesyldiphosphate (pdb code 4mbg). 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 Crystal Structure of Aspergillus Fumigatus Protein Farnesyltransferase Binary Complex with Farnesyldiphosphate, PDB code: 4mbg:

Zinc binding site 1 out of 1 in 4mbg

Go back to Zinc Binding Sites List in 4mbg
Zinc binding site 1 out of 1 in the Crystal Structure of Aspergillus Fumigatus Protein Farnesyltransferase Binary Complex with Farnesyldiphosphate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Aspergillus Fumigatus Protein Farnesyltransferase Binary Complex with Farnesyldiphosphate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn602

b:3.4
occ:0.96
 OD2 B:ASP365 2.0 4.1 1.0
NE2 B:HIS433 2.1 2.8 1.0
O B:HOH1079 2.1 4.3 1.0
SG B:CYS367 2.3 3.3 1.0
OD1 B:ASP365 2.5 2.5 1.0
CG B:ASP365 2.6 2.4 1.0
CD2 B:HIS433 3.0 3.2 1.0
CE1 B:HIS433 3.1 2.7 1.0
CB B:CYS367 3.3 2.4 1.0
CE2 B:TYR432 3.8 3.3 1.0
CB B:ASP365 4.0 2.3 1.0
O B:HOH824 4.0 17.7 1.0
N B:CYS367 4.1 1.6 1.0
CG B:HIS433 4.1 2.8 1.0
ND1 B:HIS433 4.1 2.8 0.9
CA B:CYS367 4.3 1.6 1.0
OH B:TYR432 4.4 5.8 1.0
CB B:ASP423 4.4 4.0 1.0
O B:HOH702 4.4 4.2 1.0
CG B:ASP423 4.5 4.8 1.0
CZ B:TYR432 4.6 3.6 0.9
CD2 B:TYR432 4.7 3.1 1.0
OD2 B:ASP423 4.8 6.2 1.0
CA B:ASP423 4.9 2.9 0.9
OD1 B:ASP423 4.9 3.9 1.0
O B:HOH810 5.0 13.4 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 02:19:12 2024

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