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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: Wed Aug 20 05:32:20 2025

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