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Zinc in PDB 1kzp: Protein Farnesyltransferase Complexed with A Farnesylated K-RAS4B Peptide Product

Enzymatic activity of Protein Farnesyltransferase Complexed with A Farnesylated K-RAS4B Peptide Product

All present enzymatic activity of Protein Farnesyltransferase Complexed with A Farnesylated K-RAS4B Peptide Product:
2.5.1.21;

Protein crystallography data

The structure of Protein Farnesyltransferase Complexed with A Farnesylated K-RAS4B Peptide Product, PDB code: 1kzp was solved by S.B.Long, 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) 50.00 / 2.10
Space group P 61
Cell size a, b, c (Å), α, β, γ (°) 171.239, 171.239, 69.361, 90.00, 90.00, 120.00
R / Rfree (%) 16.4 / 20.2

Zinc Binding Sites:

The binding sites of Zinc atom in the Protein Farnesyltransferase Complexed with A Farnesylated K-RAS4B Peptide Product (pdb code 1kzp). 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 K-RAS4B Peptide Product, PDB code: 1kzp:

Zinc binding site 1 out of 1 in 1kzp

Go back to Zinc Binding Sites List in 1kzp
Zinc binding site 1 out of 1 in the Protein Farnesyltransferase Complexed with A Farnesylated K-RAS4B Peptide Product


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 K-RAS4B Peptide Product within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn1001

b:26.7
occ:1.00
OD2 B:ASP297 2.1 23.4 1.0
NE2 B:HIS362 2.2 26.6 1.0
SG B:CYS299 2.3 20.0 1.0
OD1 B:ASP297 2.4 21.3 1.0
CG B:ASP297 2.5 23.5 1.0
SG C:CYS8 2.7 41.6 1.0
CD2 B:HIS362 3.1 24.4 1.0
CE1 B:HIS362 3.2 26.1 1.0
CB B:CYS299 3.3 18.4 1.0
C1 C:FAR12 3.4 43.0 1.0
C2 C:FAR12 3.5 39.3 1.0
CE2 B:TYR361 3.9 22.0 1.0
CB C:CYS8 3.9 46.7 1.0
N B:CYS299 4.0 21.7 1.0
CB B:ASP297 4.0 20.7 1.0
CG B:HIS362 4.2 24.6 1.0
ND1 B:HIS362 4.2 27.0 1.0
O B:HOH1175 4.2 49.8 1.0
CA B:CYS299 4.2 20.0 1.0
O B:HOH1573 4.4 47.3 1.0
CB B:ASP352 4.5 24.8 1.0
OH B:TYR361 4.5 20.7 1.0
CG B:ASP352 4.5 25.9 1.0
OD2 B:ASP352 4.7 29.6 1.0
CZ B:TYR361 4.7 19.8 1.0
CD2 B:TYR361 4.7 20.4 1.0
C3 C:FAR12 4.8 39.5 1.0
CA B:ASP352 4.9 24.8 1.0
OD1 B:ASP352 5.0 29.3 1.0
C B:ASP297 5.0 22.1 1.0

Reference:

S.B.Long, P.J.Casey, L.S.Beese. Reaction Path of Protein Farnesyltransferase at Atomic Resolution Nature V. 419 645 2002.
ISSN: ISSN 0028-0836
PubMed: 12374986
DOI: 10.1038/NATURE00986
Page generated: Wed Dec 16 02:55:45 2020

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