Atomistry » Chlorine » PDB 1ti7-1u33 » 1tmj
Atomistry »
  Chlorine »
    PDB 1ti7-1u33 »
      1tmj »

Chlorine in PDB 1tmj: Crystal Structure of E.Coli Apo-Hppk(W89A) at 1.45 Angstrom Resolution

Enzymatic activity of Crystal Structure of E.Coli Apo-Hppk(W89A) at 1.45 Angstrom Resolution

All present enzymatic activity of Crystal Structure of E.Coli Apo-Hppk(W89A) at 1.45 Angstrom Resolution:
2.7.6.3;

Protein crystallography data

The structure of Crystal Structure of E.Coli Apo-Hppk(W89A) at 1.45 Angstrom Resolution, PDB code: 1tmj was solved by J.Blaszczyk, X.Ji, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.45
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 36.132, 46.570, 43.365, 90.00, 110.36, 90.00
R / Rfree (%) 15.5 / 17.4

Other elements in 1tmj:

The structure of Crystal Structure of E.Coli Apo-Hppk(W89A) at 1.45 Angstrom Resolution also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of E.Coli Apo-Hppk(W89A) at 1.45 Angstrom Resolution (pdb code 1tmj). 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 Crystal Structure of E.Coli Apo-Hppk(W89A) at 1.45 Angstrom Resolution, PDB code: 1tmj:

Chlorine binding site 1 out of 1 in 1tmj

Go back to Chlorine Binding Sites List in 1tmj
Chlorine binding site 1 out of 1 in the Crystal Structure of E.Coli Apo-Hppk(W89A) at 1.45 Angstrom Resolution


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of E.Coli Apo-Hppk(W89A) at 1.45 Angstrom Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl163

b:31.8
occ:1.00
 O A:HOH337 3.1 31.8 1.0
CG A:ASP139 3.3 35.9 1.0
N A:ASP139 3.4 30.5 1.0
NZ A:LYS119 3.4 25.6 1.0
OD1 A:ASP139 3.4 26.9 1.0
CB A:ASP139 3.5 31.5 1.0
CB A:PHE137 3.6 14.8 1.0
CD A:PRO138 3.6 22.1 1.0
CG A:PRO114 3.7 22.1 1.0
O A:HOH336 3.7 39.4 1.0
OD2 A:ASP139 3.7 35.9 1.0
N A:PRO138 3.9 23.1 1.0
CE A:LYS119 4.0 17.5 1.0
CA A:ASP139 4.1 29.1 1.0
CB A:PRO138 4.2 26.0 1.0
CD A:PRO114 4.3 20.1 1.0
C A:PRO138 4.3 30.9 1.0
CD2 A:PHE137 4.3 14.0 1.0
CG A:PHE137 4.4 11.3 1.0
CG A:PRO138 4.4 24.4 1.0
C A:PHE137 4.4 20.9 1.0
CA A:PRO138 4.4 26.9 1.0
CA A:PHE137 4.6 17.7 1.0
O A:HOH379 4.6 47.2 1.0
O A:HOH301 4.6 34.0 1.0
CB A:PRO114 4.6 19.7 1.0

Reference:

Y.Li, J.Blaszczyk, Y.Wu, G.Shi, X.Ji, H.Yan. Is the Critical Role of Loop 3 of Escherichia Coli 6-Hydroxymethyl-7,8-Dihydropterin Pyrophosphokinase in Catalysis Due to Loop-3 Residues Arginine-84 and Tryptophan-89? Site-Directed Mutagenesis, Biochemical, and Crystallographic Studies. Biochemistry V. 44 8590 2005.
ISSN: ISSN 0006-2960
PubMed: 15952765
DOI: 10.1021/BI0503495
Page generated: Thu Jul 10 19:37:21 2025

Last articles

Fe in 2YXO
Fe in 2YRS
Fe in 2YXC
Fe in 2YNM
Fe in 2YVJ
Fe in 2YP1
Fe in 2YU2
Fe in 2YU1
Fe in 2YQB
Fe in 2YOO
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy