Atomistry » Zinc » PDB 2gzi-2han » 2h6f
Atomistry »
  Zinc »
    PDB 2gzi-2han »
      2h6f »

Zinc in PDB 2h6f: Protein Farnesyltransferase Complexed with A Farnesylated Ddptasacvls Peptide Product at 1.5A Resolution

Enzymatic activity of Protein Farnesyltransferase Complexed with A Farnesylated Ddptasacvls Peptide Product at 1.5A Resolution

All present enzymatic activity of Protein Farnesyltransferase Complexed with A Farnesylated Ddptasacvls Peptide Product at 1.5A Resolution:
2.5.1.58; 2.5.1.59;

Protein crystallography data

The structure of Protein Farnesyltransferase Complexed with A Farnesylated Ddptasacvls Peptide Product at 1.5A Resolution, PDB code: 2h6f was solved by K.L.Terry, L.S.Beese, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.66 / 1.50
Space group P 61
Cell size a, b, c (Å), α, β, γ (°) 178.572, 178.572, 64.660, 90.00, 90.00, 120.00
R / Rfree (%) 19 / 20.3

Zinc Binding Sites:

The binding sites of Zinc atom in the Protein Farnesyltransferase Complexed with A Farnesylated Ddptasacvls Peptide Product at 1.5A Resolution (pdb code 2h6f). 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 Protein Farnesyltransferase Complexed with A Farnesylated Ddptasacvls Peptide Product at 1.5A Resolution, PDB code: 2h6f:

Zinc binding site 1 out of 1 in 2h6f

Go back to Zinc Binding Sites List in 2h6f
Zinc binding site 1 out of 1 in the Protein Farnesyltransferase Complexed with A Farnesylated Ddptasacvls Peptide Product at 1.5A Resolution


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Protein Farnesyltransferase Complexed with A Farnesylated Ddptasacvls Peptide Product at 1.5A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn1001

b:13.1
occ:1.00
OD2 B:ASP797 2.0 13.8 1.0
NE2 B:HIS862 2.1 11.9 1.0
SG B:CYS799 2.3 11.9 1.0
OD1 B:ASP797 2.4 13.0 1.0
CG B:ASP797 2.5 13.2 1.0
SG P:CYS2006 2.7 24.7 1.0
CE1 B:HIS862 3.0 12.3 1.0
CD2 B:HIS862 3.0 11.7 1.0
CB B:CYS799 3.3 10.9 1.0
C1 P:FAR2010 3.6 24.3 1.0
CE2 B:TYR861 3.9 11.2 1.0
O B:HOH1905 4.0 31.4 1.0
CB B:ASP797 4.0 12.5 1.0
N B:CYS799 4.0 11.1 1.0
C2 P:FAR2010 4.0 24.1 1.0
CB P:CYS2006 4.0 25.6 1.0
ND1 B:HIS862 4.1 11.5 1.0
CG B:HIS862 4.1 11.3 1.0
CA B:CYS799 4.2 11.2 1.0
CB B:ASP852 4.4 14.4 1.0
CG B:ASP852 4.4 15.0 1.0
OD2 B:ASP852 4.5 17.3 1.0
O B:HOH1207 4.5 30.3 1.0
OH B:TYR861 4.6 11.4 1.0
CZ B:TYR861 4.7 11.3 1.0
CA B:ASP852 4.8 13.7 1.0
CD2 B:TYR861 4.8 11.2 1.0
C B:ASP797 4.9 11.9 1.0
CA B:ASP797 4.9 12.1 1.0
OD1 B:ASP852 5.0 15.8 1.0
CE1 B:TYR800 5.0 16.2 1.0

Reference:

K.L.Terry, P.J.Casey, L.S.Beese. Conversion of Protein Farnesyltransferase to A Geranylgeranyltransferase. Biochemistry V. 45 9746 2006.
ISSN: ISSN 0006-2960
PubMed: 16893176
DOI: 10.1021/BI060295E
Page generated: Thu Oct 17 00:32:42 2024

Last articles

Zn in 9MJ5
Zn in 9HNW
Zn in 9G0L
Zn in 9FNE
Zn in 9DZN
Zn in 9E0I
Zn in 9D32
Zn in 9DAK
Zn in 8ZXC
Zn in 8ZUF
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy