Atomistry » Chlorine » PDB 3pf6-3pne » 3pmj
Atomistry »
  Chlorine »
    PDB 3pf6-3pne »
      3pmj »

Chlorine in PDB 3pmj: Bovine Trypsin Variant X(TRIPLEILE227) in Complex with Small Molecule Inhibitor

Enzymatic activity of Bovine Trypsin Variant X(TRIPLEILE227) in Complex with Small Molecule Inhibitor

All present enzymatic activity of Bovine Trypsin Variant X(TRIPLEILE227) in Complex with Small Molecule Inhibitor:
3.4.21.4;

Protein crystallography data

The structure of Bovine Trypsin Variant X(TRIPLEILE227) in Complex with Small Molecule Inhibitor, PDB code: 3pmj was solved by A.Tziridis, P.Neumann, P.Kolenko, M.T.Stubbs, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 21.80 / 1.45
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 54.665, 54.665, 111.969, 90.00, 90.00, 120.00
R / Rfree (%) 17.6 / 23

Other elements in 3pmj:

The structure of Bovine Trypsin Variant X(TRIPLEILE227) in Complex with Small Molecule Inhibitor also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Bovine Trypsin Variant X(TRIPLEILE227) in Complex with Small Molecule Inhibitor (pdb code 3pmj). 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 Bovine Trypsin Variant X(TRIPLEILE227) in Complex with Small Molecule Inhibitor, PDB code: 3pmj:

Chlorine binding site 1 out of 1 in 3pmj

Go back to Chlorine Binding Sites List in 3pmj
Chlorine binding site 1 out of 1 in the Bovine Trypsin Variant X(TRIPLEILE227) in Complex with Small Molecule Inhibitor


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Bovine Trypsin Variant X(TRIPLEILE227) in Complex with Small Molecule Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl308

b:44.5
occ:1.00
 N A:SER166 3.2 17.7 1.0
O A:HOH1198 3.2 28.2 1.0
OG A:SER166 3.4 20.1 1.0
N A:ASP165 3.5 17.0 1.0
CB A:SER166 3.6 19.0 1.0
CB A:ASP165 3.9 18.0 1.0
CA A:SER166 4.0 18.6 1.0
CB A:SER164 4.0 17.6 1.0
O A:HOH1195 4.0 32.3 1.0
CA A:ASP165 4.0 17.7 1.0
C A:ASP165 4.1 17.6 1.0
C A:SER164 4.3 16.8 1.0
OG A:SER164 4.3 18.8 1.0
CA A:SER164 4.5 16.8 1.0
O A:HOH1032 4.8 44.2 1.0
CG A:ASP165 4.9 19.2 1.0

Reference:

A.Tziridis, D.Rauh, P.Neumann, P.Kolenko, A.Menzel, U.Brauer, C.Ursel, P.Steinmetzer, J.Sturzebecher, A.Schweinitz, T.Steinmetzer, M.T.Stubbs. Correlating Structure and Ligand Affinity in Drug Discovery: A Cautionary Tale Involving Second Shell Residues. Biol.Chem. V. 395 891 2014.
ISSN: ISSN 1431-6730
PubMed: 25003390
DOI: 10.1515/HSZ-2014-0158
Page generated: Sun Jul 21 02:30:32 2024

Last articles

Zn in 9J0N
Zn in 9J0O
Zn in 9J0P
Zn in 9FJX
Zn in 9EKB
Zn in 9C0F
Zn in 9CAH
Zn in 9CH0
Zn in 9CH3
Zn in 9CH1
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy