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Zinc in PDB 1jcr: Crystal Structure of Rat Protein Farnesyltransferase Complexed with the Non-Substrate Tetrapeptide Inhibitor Cvfm and Farnesyl Diphosphate Substrate

Protein crystallography data

The structure of Crystal Structure of Rat Protein Farnesyltransferase Complexed with the Non-Substrate Tetrapeptide Inhibitor Cvfm and Farnesyl Diphosphate Substrate, PDB code: 1jcr 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 / 2.00
Space group P 61
Cell size a, b, c (Å), α, β, γ (°) 171.225, 171.225, 69.332, 90.00, 90.00, 120.00
R / Rfree (%) 16.6 / 20.6

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Rat Protein Farnesyltransferase Complexed with the Non-Substrate Tetrapeptide Inhibitor Cvfm and Farnesyl Diphosphate Substrate (pdb code 1jcr). 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 Crystal Structure of Rat Protein Farnesyltransferase Complexed with the Non-Substrate Tetrapeptide Inhibitor Cvfm and Farnesyl Diphosphate Substrate, PDB code: 1jcr:

Zinc binding site 1 out of 1 in 1jcr

Go back to Zinc Binding Sites List in 1jcr
Zinc binding site 1 out of 1 in the Crystal Structure of Rat Protein Farnesyltransferase Complexed with the Non-Substrate Tetrapeptide Inhibitor Cvfm and Farnesyl Diphosphate Substrate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Rat Protein Farnesyltransferase Complexed with the Non-Substrate Tetrapeptide Inhibitor Cvfm and Farnesyl Diphosphate Substrate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn1001

b:28.5
occ:1.00
OD2 B:ASP297 2.1 19.4 1.0
NE2 B:HIS362 2.2 23.4 1.0
SG B:CYS299 2.3 21.5 1.0
SG C:CYS1 2.4 42.5 1.0
OD1 B:ASP297 2.5 18.1 1.0
CG B:ASP297 2.6 19.4 1.0
CE1 B:HIS362 3.1 23.6 1.0
CD2 B:HIS362 3.2 20.6 1.0
CB B:CYS299 3.4 19.9 1.0
CB C:CYS1 3.5 47.9 1.0
CE2 B:TYR361 3.8 21.3 1.0
O B:HOH1613 4.0 43.4 1.0
CB B:ASP297 4.1 18.0 1.0
N B:CYS299 4.1 20.3 1.0
ND1 B:HIS362 4.2 24.9 1.0
CG B:HIS362 4.3 22.5 1.0
O B:HOH1573 4.3 20.6 1.0
CA B:CYS299 4.3 18.3 1.0
OH B:TYR361 4.5 21.8 1.0
CG B:ASP352 4.6 24.9 1.0
CD2 B:TYR361 4.6 21.3 1.0
CB B:ASP352 4.6 22.6 1.0
CZ B:TYR361 4.6 20.8 1.0
OD2 B:ASP352 4.7 27.9 1.0
CA C:CYS1 4.8 52.1 1.0
N C:CYS1 4.8 49.0 1.0

Reference:

S.B.Long, P.J.Hancock, A.M.Kral, H.W.Hellinga, L.S.Beese. The Crystal Structure of Human Protein Farnesyltransferase Reveals the Basis For Inhibition By Caax Tetrapeptides and Their Mimetics. Proc.Natl.Acad.Sci.Usa V. 98 12948 2001.
ISSN: ISSN 0027-8424
PubMed: 11687658
DOI: 10.1073/PNAS.241407898
Page generated: Wed Dec 16 02:53:47 2020

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