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Zinc in PDB 1d8d: Co-Crystal Structure of Rat Protein Farnesyltransferase Complexed with A K-RAS4B Peptide Substrate and Fpp Analog at 2.0A Resolution

Enzymatic activity of Co-Crystal Structure of Rat Protein Farnesyltransferase Complexed with A K-RAS4B Peptide Substrate and Fpp Analog at 2.0A Resolution

All present enzymatic activity of Co-Crystal Structure of Rat Protein Farnesyltransferase Complexed with A K-RAS4B Peptide Substrate and Fpp Analog at 2.0A Resolution:
2.5.1.21;

Protein crystallography data

The structure of Co-Crystal Structure of Rat Protein Farnesyltransferase Complexed with A K-RAS4B Peptide Substrate and Fpp Analog at 2.0A Resolution, PDB code: 1d8d 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) 35.00 / 2.00
Space group P 61
Cell size a, b, c (Å), α, β, γ (°) 170.919, 170.919, 69.284, 90.00, 90.00, 120.00
R / Rfree (%) 16.4 / 20

Zinc Binding Sites:

The binding sites of Zinc atom in the Co-Crystal Structure of Rat Protein Farnesyltransferase Complexed with A K-RAS4B Peptide Substrate and Fpp Analog at 2.0A Resolution (pdb code 1d8d). 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 Co-Crystal Structure of Rat Protein Farnesyltransferase Complexed with A K-RAS4B Peptide Substrate and Fpp Analog at 2.0A Resolution, PDB code: 1d8d:

Zinc binding site 1 out of 1 in 1d8d

Go back to Zinc Binding Sites List in 1d8d
Zinc binding site 1 out of 1 in the Co-Crystal Structure of Rat Protein Farnesyltransferase Complexed with A K-RAS4B Peptide Substrate and Fpp Analog at 2.0A Resolution


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Co-Crystal Structure of Rat Protein Farnesyltransferase Complexed with A K-RAS4B Peptide Substrate and Fpp Analog at 2.0A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1001

b:23.1
occ:1.00
OD2 B:ASP297 2.0 18.4 1.0
NE2 B:HIS362 2.2 20.8 1.0
SG B:CYS299 2.3 20.1 1.0
SG P:CYS8 2.4 24.0 1.0
OD1 B:ASP297 2.6 19.1 1.0
CG B:ASP297 2.6 21.2 1.0
CE1 B:HIS362 3.1 21.2 1.0
CD2 B:HIS362 3.2 20.6 1.0
CB B:CYS299 3.4 16.1 1.0
CB P:CYS8 3.7 28.1 1.0
CE2 B:TYR361 3.8 17.4 1.0
CB B:ASP297 4.1 18.2 1.0
O B:HOH1207 4.1 19.2 1.0
O B:HOH1175 4.1 23.1 1.0
N B:CYS299 4.1 20.5 1.0
ND1 B:HIS362 4.2 24.0 1.0
CG B:HIS362 4.2 20.9 1.0
CA B:CYS299 4.3 18.4 1.0
O B:HOH1164 4.4 17.4 1.0
OH B:TYR361 4.5 18.4 1.0
CB B:ASP352 4.5 21.7 1.0
CG B:ASP352 4.5 23.0 1.0
CZ B:TYR361 4.6 18.8 1.0
CD2 B:TYR361 4.7 18.3 1.0
OD2 B:ASP352 4.7 24.6 1.0
OD1 B:ASP352 5.0 23.5 1.0
CA B:ASP352 5.0 23.0 1.0

Reference:

S.B.Long, P.J.Casey, L.S.Beese. The Basis For K-RAS4B Binding Specificity to Protein Farnesyltransferase Revealed By 2 A Resolution Ternary Complex Structures. Structure Fold.Des. V. 8 209 2000.
ISSN: ISSN 0969-2126
PubMed: 10673434
DOI: 10.1016/S0969-2126(00)00096-4
Page generated: Mon Jan 25 16:08:19 2021

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