Atomistry » Zinc » PDB 2qyn-2rgl » 2r2l
Atomistry »
  Zinc »
    PDB 2qyn-2rgl »
      2r2l »

Zinc in PDB 2r2l: Structure of Farnesyl Protein Transferase Bound to Pb-93

Enzymatic activity of Structure of Farnesyl Protein Transferase Bound to Pb-93

All present enzymatic activity of Structure of Farnesyl Protein Transferase Bound to Pb-93:
2.5.1.58;

Protein crystallography data

The structure of Structure of Farnesyl Protein Transferase Bound to Pb-93, PDB code: 2r2l was solved by C.O.Strickland, W.Voorhis, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.23
Space group P 61
Cell size a, b, c (Å), α, β, γ (°) 171.614, 171.614, 69.155, 90.00, 90.00, 120.00
R / Rfree (%) 18.9 / 22.1

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of Farnesyl Protein Transferase Bound to Pb-93 (pdb code 2r2l). 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 Farnesyl Protein Transferase Bound to Pb-93, PDB code: 2r2l:

Zinc binding site 1 out of 1 in 2r2l

Go back to Zinc Binding Sites List in 2r2l
Zinc binding site 1 out of 1 in the Structure of Farnesyl Protein Transferase Bound to Pb-93


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Farnesyl Protein Transferase Bound to Pb-93 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn1

b:38.6
occ:1.00
N65 B:PB9425 2.1 45.5 1.0
OD2 B:ASP297 2.2 24.3 1.0
NE2 B:HIS362 2.2 29.0 1.0
SG B:CYS299 2.4 30.4 1.0
OD1 B:ASP297 2.6 26.9 1.0
CG B:ASP297 2.7 22.4 1.0
C66 B:PB9425 3.1 48.7 1.0
CD2 B:HIS362 3.1 28.6 1.0
CB B:CYS299 3.2 24.7 1.0
CE1 B:HIS362 3.2 29.0 1.0
C64 B:PB9425 3.2 41.8 1.0
CE2 B:TYR361 3.8 30.7 1.0
N B:CYS299 4.1 26.3 1.0
CB B:ASP297 4.1 20.9 1.0
CG B:HIS362 4.2 31.6 1.0
CA B:CYS299 4.2 25.7 1.0
N67 B:PB9425 4.3 50.1 1.0
ND1 B:HIS362 4.3 33.0 1.0
C61 B:PB9425 4.3 46.3 1.0
O B:HOH525 4.5 36.1 1.0
CB B:ASP352 4.5 37.1 1.0
OH B:TYR361 4.5 35.0 1.0
CD2 B:TYR361 4.6 25.9 1.0
CG B:ASP352 4.6 40.5 1.0
CZ B:TYR361 4.7 32.5 1.0
OD1 B:ASP352 4.7 40.1 1.0
C27 B:PB9425 4.8 51.7 1.0
CA B:ASP352 4.8 34.0 1.0

Reference:

W.C.Van Voorhis, K.L.Rivas, P.Bendale, L.Nallan, C.Horney, L.K.Barrett, K.D.Bauer, B.P.Smart, S.Ankala, O.Hucke, C.L.Verlinde, D.Chakrabarti, C.Strickland, K.Yokoyama, F.S.Buckner, A.D.Hamilton, D.K.Williams, L.J.Lombardo, D.Floyd, M.H.Gelb. Efficacy, Pharmacokinetics, and Metabolism of Tetrahydroquinoline Inhibitors of Plasmodium Falciparum Protein Farnesyltransferase. Antimicrob.Agents Chemother. V. 51 3659 2007.
ISSN: ISSN 0066-4804
PubMed: 17606674
DOI: 10.1128/AAC.00246-07
Page generated: Thu Oct 17 03:39:17 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy