Atomistry » Zinc » PDB 1nvd-1ohl » 1o5m
Atomistry »
  Zinc »
    PDB 1nvd-1ohl »
      1o5m »

Zinc in PDB 1o5m: Structure of Fpt Bound to the Inhibitor SCH66336

Protein crystallography data

The structure of Structure of Fpt Bound to the Inhibitor SCH66336, PDB code: 1o5m was solved by C.L.Strickland, P.C.Weber, A.K.Ganguly, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 2.30
Space group P 61
Cell size a, b, c (Å), α, β, γ (°) 171.110, 171.110, 69.310, 90.00, 90.00, 120.00
R / Rfree (%) 17.4 / n/a

Other elements in 1o5m:

The structure of Structure of Fpt Bound to the Inhibitor SCH66336 also contains other interesting chemical elements:

Bromine (Br) 2 atoms
Chlorine (Cl) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of Fpt Bound to the Inhibitor SCH66336 (pdb code 1o5m). 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 Structure of Fpt Bound to the Inhibitor SCH66336, PDB code: 1o5m:

Zinc binding site 1 out of 1 in 1o5m

Go back to Zinc Binding Sites List in 1o5m
Zinc binding site 1 out of 1 in the Structure of Fpt Bound to the Inhibitor SCH66336


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Fpt Bound to the Inhibitor SCH66336 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn1001

b:24.1
occ:1.00
OD2 B:ASP297 2.0 13.9 1.0
SG B:CYS299 2.3 18.0 1.0
NE2 B:HIS362 2.3 19.4 1.0
OD1 B:ASP297 2.5 19.5 1.0
O B:HOH3388 2.5 21.8 1.0
CG B:ASP297 2.5 14.0 1.0
CD2 B:HIS362 3.1 16.7 1.0
CB B:CYS299 3.3 13.3 1.0
CE1 B:HIS362 3.3 19.9 1.0
CE2 B:TYR361 3.9 7.4 1.0
CB B:ASP297 4.0 11.7 1.0
N B:CYS299 4.0 17.7 1.0
O B:HOH3389 4.1 35.3 1.0
CA B:CYS299 4.2 13.4 1.0
CG B:HIS362 4.3 18.4 1.0
ND1 B:HIS362 4.3 22.1 1.0
O B:HOH3105 4.4 15.8 1.0
O B:HOH3380 4.4 46.9 1.0
OH B:TYR361 4.5 15.5 1.0
CB B:ASP352 4.6 20.2 1.0
CZ B:TYR361 4.7 10.2 1.0
CG B:ASP352 4.7 21.7 1.0
CD2 B:TYR361 4.7 8.6 1.0
CA B:ASP352 4.8 19.0 1.0
O B:HOH3392 5.0 55.4 1.0
OD1 B:ASP352 5.0 24.0 1.0
C B:ASP297 5.0 15.9 1.0

Reference:

C.L.Strickland, P.C.Weber, W.T.Windsor, Z.Wu, H.V.Le, M.M.Albanese, C.S.Alvarez, D.Cesarz, J.Del Rosario, J.Deskus, A.K.Mallams, F.G.Njoroge, J.J.Piwinski, S.Remiszewski, R.R.Rossman, A.G.Taveras, B.Vibulbhan, R.J.Doll, V.M.Girijavallabhan, A.K.Ganguly. Tricyclic Farnesyl Protein Transferase Inhibitors: Crystallographic and Calorimetric Studies of Structure-Activity Relationships J.Med.Chem. V. 42 2125 1999.
ISSN: ISSN 0022-2623
PubMed: 10377218
DOI: 10.1021/JM990030G
Page generated: Mon Jan 25 16:10:44 2021

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy