Atomistry » Zinc » PDB 2gzf-2h6t » 2h6h
Atomistry »
  Zinc »
    PDB 2gzf-2h6t »
      2h6h »

Zinc in PDB 2h6h: Y365F Protein Farnesyltransferase Mutant Complexed with A Farnesylated Ddptasacvls Peptide Product at 1.8A

Enzymatic activity of Y365F Protein Farnesyltransferase Mutant Complexed with A Farnesylated Ddptasacvls Peptide Product at 1.8A

All present enzymatic activity of Y365F Protein Farnesyltransferase Mutant Complexed with A Farnesylated Ddptasacvls Peptide Product at 1.8A:
2.5.1.58; 2.5.1.59;

Protein crystallography data

The structure of Y365F Protein Farnesyltransferase Mutant Complexed with A Farnesylated Ddptasacvls Peptide Product at 1.8A, PDB code: 2h6h 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) 49.59 / 1.80
Space group P 61
Cell size a, b, c (Å), α, β, γ (°) 178.782, 178.782, 64.587, 90.00, 90.00, 120.00
R / Rfree (%) 17.7 / 18

Zinc Binding Sites:

The binding sites of Zinc atom in the Y365F Protein Farnesyltransferase Mutant Complexed with A Farnesylated Ddptasacvls Peptide Product at 1.8A (pdb code 2h6h). 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 Y365F Protein Farnesyltransferase Mutant Complexed with A Farnesylated Ddptasacvls Peptide Product at 1.8A, PDB code: 2h6h:

Zinc binding site 1 out of 1 in 2h6h

Go back to Zinc Binding Sites List in 2h6h
Zinc binding site 1 out of 1 in the Y365F Protein Farnesyltransferase Mutant Complexed with A Farnesylated Ddptasacvls Peptide Product at 1.8A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Y365F Protein Farnesyltransferase Mutant Complexed with A Farnesylated Ddptasacvls Peptide Product at 1.8A within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn1001

b:16.7
occ:1.00
 OD2 B:ASP797 2.1 13.4 1.0
NE2 B:HIS862 2.1 13.7 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 13.3 1.0
SG P:CYS2006 2.6 19.4 1.0
CD2 B:HIS862 3.0 14.1 1.0
CE1 B:HIS862 3.1 14.0 1.0
CB B:CYS799 3.2 11.8 1.0
C1 P:FAR2010 3.4 19.9 1.0
CB P:CYS2006 3.8 21.9 1.0
CE2 B:TYR861 3.9 11.6 1.0
C2 P:FAR2010 3.9 19.3 1.0
CB B:ASP797 4.0 12.8 1.0
N B:CYS799 4.0 11.1 1.0
OG P:SER2004 4.2 30.1 1.0
ND1 B:HIS862 4.2 13.2 1.0
CG B:HIS862 4.2 13.0 1.0
CA B:CYS799 4.2 11.6 1.0
OD2 B:ASP852 4.3 18.5 1.0
O B:HOH1207 4.4 32.5 1.0
CG B:ASP852 4.4 16.9 1.0
OH B:TYR861 4.5 12.7 1.0
CB B:ASP852 4.5 16.0 1.0
CZ B:TYR861 4.7 12.1 1.0
CD2 B:TYR861 4.7 11.4 1.0
CA B:ASP852 4.8 15.7 1.0
OD1 B:ASP852 4.9 17.4 1.0
CA B:ASP797 5.0 12.8 1.0
C B:ASP797 5.0 12.4 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 00:33:01 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy