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Zinc in PDB 3pz4: Crystal Structure of Ftase(Alpha-Subunit; Beta-Subunit Delta C10) in Complex with BMS3 and Lipid Substrate Fpp

Enzymatic activity of Crystal Structure of Ftase(Alpha-Subunit; Beta-Subunit Delta C10) in Complex with BMS3 and Lipid Substrate Fpp

All present enzymatic activity of Crystal Structure of Ftase(Alpha-Subunit; Beta-Subunit Delta C10) in Complex with BMS3 and Lipid Substrate Fpp:
2.5.1.58; 2.5.1.59;

Protein crystallography data

The structure of Crystal Structure of Ftase(Alpha-Subunit; Beta-Subunit Delta C10) in Complex with BMS3 and Lipid Substrate Fpp, PDB code: 3pz4 was solved by Z.Guo, R.S.Bon, E.A.Stigter, H.Waldmann, K.Alexandrov, W.Blankenfeldt, R.S.Goody, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.91 / 2.10
Space group P 61
Cell size a, b, c (Å), α, β, γ (°) 170.746, 170.746, 69.085, 90.00, 90.00, 120.00
R / Rfree (%) 22.5 / 26.7

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Ftase(Alpha-Subunit; Beta-Subunit Delta C10) in Complex with BMS3 and Lipid Substrate Fpp (pdb code 3pz4). 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 Ftase(Alpha-Subunit; Beta-Subunit Delta C10) in Complex with BMS3 and Lipid Substrate Fpp, PDB code: 3pz4:

Zinc binding site 1 out of 1 in 3pz4

Go back to Zinc Binding Sites List in 3pz4
Zinc binding site 1 out of 1 in the Crystal Structure of Ftase(Alpha-Subunit; Beta-Subunit Delta C10) in Complex with BMS3 and Lipid Substrate Fpp


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 Ftase(Alpha-Subunit; Beta-Subunit Delta C10) in Complex with BMS3 and Lipid Substrate Fpp within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn1

b:24.4
occ:1.00
 OD2 B:ASP297 2.1 22.0 1.0
N3 B:3PZ429 2.1 26.3 1.0
NE2 B:HIS362 2.2 20.2 1.0
OD1 B:ASP297 2.3 22.1 1.0
SG B:CYS299 2.3 21.7 1.0
CG B:ASP297 2.5 21.8 1.0
C13 B:3PZ429 2.8 26.1 1.0
CD2 B:HIS362 3.1 20.6 1.0
CE1 B:HIS362 3.2 19.9 1.0
CB B:CYS299 3.2 20.2 1.0
C12 B:3PZ429 3.3 25.2 1.0
CB B:ASP297 3.9 22.7 1.0
N B:CYS299 4.0 20.7 1.0
CE2 B:TYR361 4.0 19.4 1.0
N4 B:3PZ429 4.0 28.3 1.0
C4 B:FPP428 4.0 31.5 1.0
CB B:ASP352 4.2 25.2 1.0
CA B:CYS299 4.2 20.5 1.0
ND1 B:HIS362 4.3 19.1 1.0
C11 B:3PZ429 4.3 22.5 1.0
CG B:HIS362 4.3 20.7 1.0
CG B:ASP352 4.3 24.0 1.0
OD2 B:ASP352 4.4 27.6 1.0
O B:HOH453 4.4 28.0 1.0
CA B:ASP352 4.6 25.8 1.0
OH B:TYR361 4.7 20.4 1.0
CD2 B:TYR361 4.7 20.7 1.0
OD1 B:ASP352 4.9 26.2 1.0
N B:GLY298 4.9 20.7 1.0
C B:ASP297 4.9 23.6 1.0
CA B:ASP297 4.9 24.3 1.0
CZ B:TYR361 4.9 20.2 1.0

Reference:

R.S.Bon, Z.Guo, E.A.Stigter, S.Wetzel, S.Menninger, A.Wolf, A.Choidas, K.Alexandrov, W.Blankenfeldt, R.S.Goody, H.Waldmann. Structure-Guided Development of Selective Rabggtase Inhibitors. Angew.Chem.Int.Ed.Engl. V. 50 4957 2011.
ISSN: ISSN 1433-7851
PubMed: 21520375
DOI: 10.1002/ANIE.201101210
Page generated: Wed Dec 16 04:44:16 2020

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