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Zinc in PDB 1tn8: Protein Farnesyltransferase Complexed with A H-Ras Peptide Substrate and A Fpp Analog at 2.25A Resolution

Enzymatic activity of Protein Farnesyltransferase Complexed with A H-Ras Peptide Substrate and A Fpp Analog at 2.25A Resolution

All present enzymatic activity of Protein Farnesyltransferase Complexed with A H-Ras Peptide Substrate and A Fpp Analog at 2.25A Resolution:
2.5.1.58;

Protein crystallography data

The structure of Protein Farnesyltransferase Complexed with A H-Ras Peptide Substrate and A Fpp Analog at 2.25A Resolution, PDB code: 1tn8 was solved by T.S.Reid, K.L.Terry, P.J.Casey, L.S.Beese, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 37.06 / 2.25
Space group P 61
Cell size a, b, c (Å), α, β, γ (°) 171.147, 171.147, 69.326, 90.00, 90.00, 120.00
R / Rfree (%) 19.3 / 21.8

Zinc Binding Sites:

The binding sites of Zinc atom in the Protein Farnesyltransferase Complexed with A H-Ras Peptide Substrate and A Fpp Analog at 2.25A Resolution (pdb code 1tn8). 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 H-Ras Peptide Substrate and A Fpp Analog at 2.25A Resolution, PDB code: 1tn8:

Zinc binding site 1 out of 1 in 1tn8

Go back to Zinc Binding Sites List in 1tn8
Zinc binding site 1 out of 1 in the Protein Farnesyltransferase Complexed with A H-Ras Peptide Substrate and A Fpp Analog at 2.25A 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 H-Ras Peptide Substrate and A Fpp Analog at 2.25A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn1001

b:26.0
occ:1.00
 OD1 B:ASP797 2.0 18.1 1.0
NE2 B:HIS862 2.2 27.7 1.0
SG B:CYS799 2.3 26.2 1.0
SG C:CYS2006 2.4 50.1 1.0
CG B:ASP797 2.6 20.3 1.0
OD2 B:ASP797 2.6 18.8 1.0
CD2 B:HIS862 3.1 27.1 1.0
CE1 B:HIS862 3.2 27.0 1.0
CB B:CYS799 3.3 20.8 1.0
CB C:CYS2006 3.8 63.9 1.0
CE2 B:TYR861 3.8 28.4 1.0
CB B:ASP797 4.1 20.8 1.0
N B:CYS799 4.1 22.9 1.0
O B:HOH1175 4.1 42.6 1.0
CG B:HIS862 4.2 27.9 1.0
O B:HOH1207 4.2 37.1 1.0
ND1 B:HIS862 4.2 26.8 1.0
CA B:CYS799 4.3 23.3 1.0
O B:HOH1585 4.4 27.4 1.0
OH B:TYR861 4.5 27.5 1.0
CB B:ASP852 4.6 28.2 1.0
CG B:ASP852 4.6 28.9 1.0
CD2 B:TYR861 4.6 26.8 1.0
OD2 B:ASP852 4.6 31.3 1.0
CZ B:TYR861 4.6 27.4 1.0
CA B:ASP852 4.9 29.4 1.0
CA C:CYS2006 5.0 66.6 1.0

Reference:

T.S.Reid, K.L.Terry, P.J.Casey, L.S.Beese. Crystallographic Analysis of Caax Prenyltransferases Complexed with Substrates Defines Rules of Protein Substrate Selectivity. J.Mol.Biol. V. 343 417 2004.
ISSN: ISSN 0022-2836
PubMed: 15451670
DOI: 10.1016/J.JMB.2004.08.056
Page generated: Wed Oct 16 19:11:49 2024

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