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Zinc in PDB 1qbq: Structure of Rat Farnesyl Protein Transferase Complexed with A Cvim Peptide and Alpha-Hydroxyfarnesylphosphonic Acid.

Protein crystallography data

The structure of Structure of Rat Farnesyl Protein Transferase Complexed with A Cvim Peptide and Alpha-Hydroxyfarnesylphosphonic Acid., PDB code: 1qbq was solved by C.L.Strickland, W.T.Windsor, R.Syto, L.Wang, R.Bond, Z.Wu, J.Schwartz, H.V.Le, L.S.Beese, P.C.Weber, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 15.00 / 2.40
Space group P 61
Cell size a, b, c (Å), α, β, γ (°) 174.132, 174.132, 69.705, 90.00, 90.00, 120.00
R / Rfree (%) 21.8 / 29.2

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of Rat Farnesyl Protein Transferase Complexed with A Cvim Peptide and Alpha-Hydroxyfarnesylphosphonic Acid. (pdb code 1qbq). 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 Structure of Rat Farnesyl Protein Transferase Complexed with A Cvim Peptide and Alpha-Hydroxyfarnesylphosphonic Acid., PDB code: 1qbq:

Zinc binding site 1 out of 1 in 1qbq

Go back to Zinc Binding Sites List in 1qbq
Zinc binding site 1 out of 1 in the Structure of Rat Farnesyl Protein Transferase Complexed with A Cvim Peptide and Alpha-Hydroxyfarnesylphosphonic Acid.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Rat Farnesyl Protein Transferase Complexed with A Cvim Peptide and Alpha-Hydroxyfarnesylphosphonic Acid. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn1000

b:30.5
occ:1.00
OD2 B:ASP297 1.9 22.8 1.0
SG B:CYS299 2.2 25.3 1.0
NE2 B:HIS362 2.2 22.1 1.0
OD1 B:ASP297 2.5 25.0 1.0
CG B:ASP297 2.5 22.2 1.0
SG P:CYS1 2.5 41.2 1.0
CD2 B:HIS362 3.0 21.8 1.0
CE1 B:HIS362 3.3 28.0 1.0
CB B:CYS299 3.3 19.8 1.0
CB P:CYS1 3.8 42.3 1.0
CE2 B:TYR361 3.9 17.2 1.0
N B:CYS299 3.9 27.0 1.0
CB B:ASP297 3.9 24.4 1.0
CA B:CYS299 4.2 23.5 1.0
CG B:HIS362 4.2 21.9 1.0
ND1 B:HIS362 4.3 24.2 1.0
OH B:TYR361 4.5 20.6 1.0
OD2 B:ASP352 4.5 33.5 1.0
O B:HOH1196 4.5 46.7 1.0
CG B:ASP352 4.5 30.5 1.0
O B:HOH1224 4.6 40.5 1.0
CB B:ASP352 4.6 29.3 1.0
CZ B:TYR361 4.7 15.3 1.0
CD2 B:TYR361 4.7 15.2 1.0
CE1 B:TYR300 4.8 35.9 1.0
C B:ASP297 4.9 26.6 1.0
CA B:ASP352 4.9 28.4 1.0
CA B:ASP297 4.9 24.4 1.0
N B:GLY298 4.9 28.9 1.0
CD1 B:TYR300 4.9 32.5 1.0

Reference:

C.L.Strickland, W.T.Windsor, R.Syto, L.Wang, R.Bond, Z.Wu, J.Schwartz, H.V.Le, L.S.Beese, P.C.Weber. Crystal Structure of Farnesyl Protein Transferase Complexed with A Caax Peptide and Farnesyl Diphosphate Analogue Biochemistry V. 37 16601 1998.
ISSN: ISSN 0006-2960
PubMed: 9843427
DOI: 10.1021/BI981197Z
Page generated: Mon Jan 25 16:11:58 2021

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