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Caesium in PDB 1q6u: Crystal Structure of Fkpa From Escherichia Coli

Enzymatic activity of Crystal Structure of Fkpa From Escherichia Coli

All present enzymatic activity of Crystal Structure of Fkpa From Escherichia Coli:
5.2.1.8;

Protein crystallography data

The structure of Crystal Structure of Fkpa From Escherichia Coli, PDB code: 1q6u was solved by F.A.Saul, J.-P.Arie, B.Vulliez-Le Normand, R.Kahn, J.-M.Betton, G.A.Bentley, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.45
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 115.180, 132.750, 41.780, 90.00, 90.00, 90.00
R / Rfree (%) 21.1 / 27.7

Caesium Binding Sites:

The binding sites of Caesium atom in the Crystal Structure of Fkpa From Escherichia Coli (pdb code 1q6u). This binding sites where shown within 5.0 Angstroms radius around Caesium atom.
In total only one binding site of Caesium was determined in the Crystal Structure of Fkpa From Escherichia Coli, PDB code: 1q6u:

Caesium binding site 1 out of 1 in 1q6u

Go back to Caesium Binding Sites List in 1q6u
Caesium binding site 1 out of 1 in the Crystal Structure of Fkpa From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Caesium with other atoms in the Cs binding site number 1 of Crystal Structure of Fkpa From Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cs246

b:36.8
occ:1.00
O A:ALA111 3.0 24.2 1.0
O A:VAL116 3.0 20.5 1.0
O A:GLU113 3.1 22.8 1.0
O A:HOH347 3.4 57.7 1.0
C A:VAL116 4.1 22.7 1.0
N A:VAL116 4.1 23.4 1.0
C A:ALA111 4.1 27.5 1.0
C A:GLU113 4.2 25.0 1.0
O A:HOH251 4.3 27.1 1.0
C A:LYS112 4.3 29.7 1.0
N A:GLU113 4.4 28.2 1.0
CA A:VAL116 4.4 23.3 1.0
CA A:LYS112 4.5 29.7 1.0
CB A:VAL116 4.5 23.2 1.0
O A:LYS112 4.6 30.6 1.0
N A:LYS112 4.8 27.9 1.0
N A:GLY115 4.9 24.7 1.0
CA A:GLU113 5.0 28.6 1.0

Reference:

F.A.Saul, J.P.Arie, B.Vulliez-Le Normand, R.Kahn, J.M.Betton, G.A.Bentley. Structural and Functional Studies of Fkpa From Escherichia Coli, A Cis/Trans Peptidyl-Prolyl Isomerase with Chaperone Activity. J.Mol.Biol. V. 335 595 2004.
ISSN: ISSN 0022-2836
PubMed: 14672666
DOI: 10.1016/J.JMB.2003.10.056
Page generated: Sun Dec 13 10:55:31 2020

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