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Zinc in PDB 2f0y: Crystal Structure of Human Protein Farnesyltransferase Complexed with Farnesyl Diphosphate and Hydantoin Derivative

Enzymatic activity of Crystal Structure of Human Protein Farnesyltransferase Complexed with Farnesyl Diphosphate and Hydantoin Derivative

All present enzymatic activity of Crystal Structure of Human Protein Farnesyltransferase Complexed with Farnesyl Diphosphate and Hydantoin Derivative:
2.5.1.58; 2.5.1.59;

Protein crystallography data

The structure of Crystal Structure of Human Protein Farnesyltransferase Complexed with Farnesyl Diphosphate and Hydantoin Derivative, PDB code: 2f0y was solved by K.H.Kim, J.Lee, J.Kim, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.70
Space group P 61
Cell size a, b, c (Å), α, β, γ (°) 171.888, 171.888, 71.367, 90.00, 90.00, 120.00
R / Rfree (%) 21.2 / 25.8

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Human Protein Farnesyltransferase Complexed with Farnesyl Diphosphate and Hydantoin Derivative (pdb code 2f0y). 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 Human Protein Farnesyltransferase Complexed with Farnesyl Diphosphate and Hydantoin Derivative, PDB code: 2f0y:

Zinc binding site 1 out of 1 in 2f0y

Go back to Zinc Binding Sites List in 2f0y
Zinc binding site 1 out of 1 in the Crystal Structure of Human Protein Farnesyltransferase Complexed with Farnesyl Diphosphate and Hydantoin Derivative


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 Human Protein Farnesyltransferase Complexed with Farnesyl Diphosphate and Hydantoin Derivative within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn501

b:66.5
occ:1.00
 OD2 B:ASP297 2.0 46.5 1.0
N5 B:3MN963 2.3 66.5 1.0
NE2 B:HIS362 2.3 45.1 1.0
SG B:CYS299 2.3 52.9 1.0
CG B:ASP297 2.6 46.5 1.0
OD1 B:ASP297 2.8 46.5 1.0
CD2 B:HIS362 3.1 45.1 1.0
C30 B:3MN963 3.2 66.5 1.0
CE1 B:HIS362 3.3 45.1 1.0
C29 B:3MN963 3.3 66.5 1.0
CB B:CYS299 3.4 52.9 1.0
CE2 B:TYR361 3.7 45.1 1.0
CB B:ASP297 4.0 46.5 1.0
O B:HOH1011 4.2 70.1 1.0
OH B:TYR361 4.2 45.1 1.0
N B:CYS299 4.3 38.9 1.0
CG B:HIS362 4.3 45.1 1.0
ND1 B:HIS362 4.3 45.1 1.0
C21 B:3MN963 4.4 66.5 1.0
CA B:CYS299 4.4 38.9 1.0
N4 B:3MN963 4.5 66.5 1.0
CZ B:TYR361 4.5 45.1 1.0
CD2 B:TYR361 4.7 45.1 1.0
O1 B:3MN963 4.8 66.5 1.0
CG B:ASP352 4.8 52.9 1.0
OD2 B:ASP352 4.9 52.9 1.0
CB B:ASP352 4.9 52.9 1.0
CZ B:TYR300 5.0 53.0 1.0

Reference:

J.Lee, J.Kim, J.S.Koh, H.H.Chung, S.Ro, K.H.Kim. Hydantoin Derivatives As Non-Pepridic Inhibitors of Ras Farnesyl Transferase To Be Published.
Page generated: Wed Oct 16 23:36:35 2024

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