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Zinc in PDB 1kzo: Protein Farnesyltransferase Complexed with Farnesylated K-RAS4B Peptide Product and Farnesyl Diphosphate Substrate Bound Simultaneously

Enzymatic activity of Protein Farnesyltransferase Complexed with Farnesylated K-RAS4B Peptide Product and Farnesyl Diphosphate Substrate Bound Simultaneously

All present enzymatic activity of Protein Farnesyltransferase Complexed with Farnesylated K-RAS4B Peptide Product and Farnesyl Diphosphate Substrate Bound Simultaneously:
2.5.1.21;

Protein crystallography data

The structure of Protein Farnesyltransferase Complexed with Farnesylated K-RAS4B Peptide Product and Farnesyl Diphosphate Substrate Bound Simultaneously, PDB code: 1kzo 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 / 2.20
Space group P 61
Cell size a, b, c (Å), α, β, γ (°) 171.199, 171.199, 69.444, 90.00, 90.00, 120.00
R / Rfree (%) 15.9 / 20.4

Zinc Binding Sites:

The binding sites of Zinc atom in the Protein Farnesyltransferase Complexed with Farnesylated K-RAS4B Peptide Product and Farnesyl Diphosphate Substrate Bound Simultaneously (pdb code 1kzo). 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 Farnesylated K-RAS4B Peptide Product and Farnesyl Diphosphate Substrate Bound Simultaneously, PDB code: 1kzo:

Zinc binding site 1 out of 1 in 1kzo

Go back to Zinc Binding Sites List in 1kzo
Zinc binding site 1 out of 1 in the Protein Farnesyltransferase Complexed with Farnesylated K-RAS4B Peptide Product and Farnesyl Diphosphate Substrate Bound Simultaneously


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 Farnesylated K-RAS4B Peptide Product and Farnesyl Diphosphate Substrate Bound Simultaneously within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn1001

b:32.6
occ:1.00
 OD2 B:ASP297 2.1 21.8 1.0
NE2 B:HIS362 2.2 21.0 1.0
SG B:CYS299 2.3 22.4 1.0
OD1 B:ASP297 2.4 18.8 1.0
CG B:ASP297 2.6 23.5 1.0
O B:HOH3212 2.7 30.6 1.0
CE1 B:HIS362 3.2 18.1 1.0
CD2 B:HIS362 3.2 19.2 1.0
CB B:CYS299 3.3 17.1 1.0
O B:HOH3185 3.5 61.7 1.0
CE2 B:TYR361 3.8 19.8 1.0
N B:CYS299 4.0 19.0 1.0
CB B:ASP297 4.0 20.0 1.0
ND1 B:HIS362 4.3 22.0 1.0
CA B:CYS299 4.3 17.2 1.0
CG B:HIS362 4.3 21.7 1.0
OH B:TYR361 4.5 20.6 1.0
O B:HOH3176 4.5 20.8 1.0
CG B:ASP352 4.6 24.7 1.0
CB B:ASP352 4.6 23.2 1.0
CZ B:TYR361 4.7 19.4 1.0
CD2 B:TYR361 4.7 17.9 1.0
OD2 B:ASP352 4.8 28.0 1.0
OD1 B:ASP352 4.8 29.6 1.0
CA B:ASP352 5.0 24.8 1.0

Reference:

S.B.Long, P.J.Casey, L.S.Beese. The 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: Sun Oct 13 04:44:07 2024

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