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Bromine in PDB 4k88: Crystal Structure of Human Prolyl-Trna Synthetase (Halofuginone Bound Form)

Enzymatic activity of Crystal Structure of Human Prolyl-Trna Synthetase (Halofuginone Bound Form)

All present enzymatic activity of Crystal Structure of Human Prolyl-Trna Synthetase (Halofuginone Bound Form):
6.1.1.15;

Protein crystallography data

The structure of Crystal Structure of Human Prolyl-Trna Synthetase (Halofuginone Bound Form), PDB code: 4k88 was solved by K.Y.Hwang, J.H.Son, E.H.Lee, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.02 / 2.62
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 120.813, 120.813, 104.711, 90.00, 90.00, 120.00
R / Rfree (%) 23.7 / 27.6

Other elements in 4k88:

The structure of Crystal Structure of Human Prolyl-Trna Synthetase (Halofuginone Bound Form) also contains other interesting chemical elements:

Chlorine (Cl) 1 atom
Zinc (Zn) 1 atom

Bromine Binding Sites:

The binding sites of Bromine atom in the Crystal Structure of Human Prolyl-Trna Synthetase (Halofuginone Bound Form) (pdb code 4k88). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total only one binding site of Bromine was determined in the Crystal Structure of Human Prolyl-Trna Synthetase (Halofuginone Bound Form), PDB code: 4k88:

Bromine binding site 1 out of 1 in 4k88

Go back to Bromine Binding Sites List in 4k88
Bromine binding site 1 out of 1 in the Crystal Structure of Human Prolyl-Trna Synthetase (Halofuginone Bound Form)


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Crystal Structure of Human Prolyl-Trna Synthetase (Halofuginone Bound Form) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br602

b:0.5
occ:1.00
 BR1 A:HFG602 0.0 0.5 1.0
C7 A:HFG602 1.9 90.5 1.0
C8 A:HFG602 2.8 84.6 1.0
C6 A:HFG602 2.9 85.4 1.0
O A:PHE97 3.1 0.3 1.0
CL1 A:HFG602 3.2 94.1 1.0
CG1 A:VAL101 3.4 80.8 1.0
CB A:PHE97 3.5 99.9 1.0
C A:PHE97 3.8 0.5 1.0
CB A:PRO120 3.9 71.2 1.0
CB A:GLU100 3.9 91.8 1.0
C9 A:HFG602 4.1 82.5 1.0
C A:GLU100 4.1 95.4 1.0
C5 A:HFG602 4.1 78.2 1.0
N A:VAL101 4.2 91.8 1.0
CA A:PHE97 4.3 0.0 1.0
CG A:PRO120 4.3 71.4 1.0
O A:GLU100 4.4 93.2 1.0
CA A:GLU100 4.5 97.3 1.0
OE2 A:GLU100 4.6 90.5 1.0
C10 A:HFG602 4.6 79.5 1.0
CB A:VAL101 4.6 80.2 1.0
CG A:PHE97 4.7 98.8 1.0
CA A:VAL101 4.7 86.9 1.0
CG A:ARG152 4.7 65.8 1.0
N A:ALA98 4.7 0.6 1.0
N A:GLU100 4.7 0.2 1.0
CD A:GLU100 4.9 94.0 1.0
CG A:GLU100 4.9 88.9 1.0
CB A:ARG152 4.9 68.9 1.0

Reference:

J.Son, E.H.Lee, M.Park, J.H.Kim, J.Kim, S.Kim, Y.H.Jeon, K.Y.Hwang. Conformational Changes in Human Prolyl-Trna Synthetase Upon Binding of the Substrates Proline and Atp and the Inhibitor Halofuginone Acta Crystallogr.,Sect.D V. 69 2136 2013.
ISSN: ISSN 0907-4449
DOI: 10.1107/S0907444913020556
Page generated: Wed Jul 10 21:44:31 2024

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