Atomistry » Chlorine » PDB 3qvp-3r40 » 3qx5
Atomistry »
  Chlorine »
    PDB 3qvp-3r40 »
      3qx5 »

Chlorine in PDB 3qx5: Thrombin Inhibition By Pyridin Derivatives

Enzymatic activity of Thrombin Inhibition By Pyridin Derivatives

All present enzymatic activity of Thrombin Inhibition By Pyridin Derivatives:
3.4.21.5;

Protein crystallography data

The structure of Thrombin Inhibition By Pyridin Derivatives, PDB code: 3qx5 was solved by A.Biela, A.Heine, G.Klebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.76 / 1.35
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 70.200, 71.100, 72.800, 90.00, 100.60, 90.00
R / Rfree (%) 13.2 / 15.6

Other elements in 3qx5:

The structure of Thrombin Inhibition By Pyridin Derivatives also contains other interesting chemical elements:

Sodium (Na) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Thrombin Inhibition By Pyridin Derivatives (pdb code 3qx5). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Thrombin Inhibition By Pyridin Derivatives, PDB code: 3qx5:

Chlorine binding site 1 out of 1 in 3qx5

Go back to Chlorine Binding Sites List in 3qx5
Chlorine binding site 1 out of 1 in the Thrombin Inhibition By Pyridin Derivatives


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Thrombin Inhibition By Pyridin Derivatives within 5.0Å range:
probe atom residue distance (Å) B Occ
H:Cl5

b:12.4
occ:1.00
CL2 H:02P5 0.0 12.4 1.0
C23 H:02P5 1.8 12.8 1.0
C24 H:02P5 2.7 14.9 1.0
C22 H:02P5 2.8 13.2 1.0
O H:TRP215 3.4 9.7 1.0
O H:PHE227 3.4 8.0 1.0
N H:PHE227 3.6 7.9 1.0
CG1 H:VAL213 3.7 9.5 1.0
CA H:GLY226 3.7 9.8 1.0
N H:TRP215 3.9 8.9 1.0
CB H:ALA190 3.9 11.8 1.0
C H:TRP215 4.0 9.3 1.0
CZ H:TYR228 4.0 8.7 1.0
N H:SER214 4.0 7.5 1.0
C H:GLY226 4.0 8.4 1.0
C25 H:02P5 4.0 14.9 1.0
C20 H:02P5 4.1 14.1 1.0
OH H:TYR228 4.1 10.2 1.0
C H:PHE227 4.2 7.7 1.0
CE2 H:TYR228 4.2 8.9 1.0
CE1 H:TYR228 4.3 7.9 1.0
OD1 H:ASP189 4.4 10.8 1.0
CA H:TRP215 4.4 9.3 1.0
C H:SER214 4.5 8.3 1.0
CA H:VAL213 4.5 7.0 1.0
N21 H:02P5 4.5 14.6 1.0
CA H:PHE227 4.5 7.7 1.0
C H:VAL213 4.6 7.2 1.0
CB H:VAL213 4.6 7.9 1.0
N H:GLY216 4.7 11.0 1.0
CD2 H:TYR228 4.7 7.5 1.0
O H:HOH1147 4.8 11.9 1.0
CD1 H:TYR228 4.8 7.6 1.0
CA H:SER214 4.8 7.7 1.0
CA H:ALA190 5.0 11.5 1.0

Reference:

A.Biela, M.Khayat, H.Tan, J.Kong, A.Heine, D.Hangauer, G.Klebe. Impact of Ligand and Protein Desolvation on Ligand Binding to the S1 Pocket of Thrombin J.Mol.Biol. V. 418 350 2012.
ISSN: ISSN 0022-2836
PubMed: 22366545
DOI: 10.1016/J.JMB.2012.01.054
Page generated: Sun Jul 21 03:17:03 2024

Last articles

Zn in 9MJ5
Zn in 9HNW
Zn in 9G0L
Zn in 9FNE
Zn in 9DZN
Zn in 9E0I
Zn in 9D32
Zn in 9DAK
Zn in 8ZXC
Zn in 8ZUF
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy