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Chlorine in PDB 2htx: Crystal Structure Analysis of Hen Egg White Lysozyme Crosslinked By Polymerized Glutaraldehyde in Acidic Environment

Enzymatic activity of Crystal Structure Analysis of Hen Egg White Lysozyme Crosslinked By Polymerized Glutaraldehyde in Acidic Environment

All present enzymatic activity of Crystal Structure Analysis of Hen Egg White Lysozyme Crosslinked By Polymerized Glutaraldehyde in Acidic Environment:
3.2.1.17;

Protein crystallography data

The structure of Crystal Structure Analysis of Hen Egg White Lysozyme Crosslinked By Polymerized Glutaraldehyde in Acidic Environment, PDB code: 2htx was solved by Y.Wine, N.Cohen-Hadar, A.Freeman, S.Lagziel-Simis, F.Frolow, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 55.73 / 1.56
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 78.856, 78.856, 36.954, 90.00, 90.00, 90.00
R / Rfree (%) 12.7 / 18.2

Other elements in 2htx:

The structure of Crystal Structure Analysis of Hen Egg White Lysozyme Crosslinked By Polymerized Glutaraldehyde in Acidic Environment also contains other interesting chemical elements:

Sodium (Na) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure Analysis of Hen Egg White Lysozyme Crosslinked By Polymerized Glutaraldehyde in Acidic Environment (pdb code 2htx). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure Analysis of Hen Egg White Lysozyme Crosslinked By Polymerized Glutaraldehyde in Acidic Environment, PDB code: 2htx:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 2htx

Go back to Chlorine Binding Sites List in 2htx
Chlorine binding site 1 out of 2 in the Crystal Structure Analysis of Hen Egg White Lysozyme Crosslinked By Polymerized Glutaraldehyde in Acidic Environment


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure Analysis of Hen Egg White Lysozyme Crosslinked By Polymerized Glutaraldehyde in Acidic Environment within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl9501

b:32.0
occ:1.00
 O A:HOH9610 3.1 24.0 1.0
N A:THR69 3.2 24.4 1.0
O A:THR69 3.3 28.0 1.0
O A:HOH9697 3.4 30.0 0.5
NA A:NA9604 3.5 60.6 1.0
N A:ARG68 3.5 22.2 1.0
OD1 A:ASN65 3.6 28.3 1.0
C A:GLY67 3.6 24.7 1.0
OG A:SER72 3.6 31.5 1.0
C A:THR69 3.6 24.8 1.0
N A:GLY67 3.7 23.4 1.0
CA A:GLY67 3.7 25.7 1.0
CA A:THR69 3.9 23.6 1.0
O A:HOH9704 4.0 31.4 1.0
C A:ARG68 4.2 27.0 1.0
CB A:THR69 4.2 24.2 1.0
O A:GLY67 4.2 30.7 1.0
OD1 A:ASP66 4.3 21.3 1.0
CA A:ARG68 4.3 23.9 0.5
CA A:ARG68 4.3 23.9 0.5
N A:PRO70 4.5 26.9 1.0
O A:HOH9705 4.7 20.3 1.0
C A:ASP66 4.8 21.7 1.0
CG A:ASN65 4.8 23.5 1.0
OG1 A:THR69 4.8 22.4 1.0
N A:ASP66 4.8 19.8 1.0
O A:HOH9630 4.9 38.5 0.5
CB A:SER72 4.9 30.4 1.0

Chlorine binding site 2 out of 2 in 2htx

Go back to Chlorine Binding Sites List in 2htx
Chlorine binding site 2 out of 2 in the Crystal Structure Analysis of Hen Egg White Lysozyme Crosslinked By Polymerized Glutaraldehyde in Acidic Environment


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure Analysis of Hen Egg White Lysozyme Crosslinked By Polymerized Glutaraldehyde in Acidic Environment within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl9502

b:67.3
occ:1.00
 O A:HOH9702 2.7 30.3 0.5
O A:HOH9626 2.9 30.8 1.0
O A:HOH9612 3.2 28.0 1.0
O A:GLU35 3.2 19.2 1.0
O A:HOH9666 4.0 47.1 1.0
O A:PHE34 4.0 23.1 1.0
C A:GLU35 4.0 18.4 1.0
OE1 A:GLU35 4.1 21.2 1.0
ND2 A:ASN44 4.2 29.0 1.0
CA A:GLU35 4.2 17.0 1.0
O A:HOH9702 4.3 24.4 0.5
OE1 A:GLN57 4.4 18.3 1.0
CG A:GLN57 4.7 17.4 1.0
CG A:ASN44 4.8 27.1 1.0
CD A:GLN57 4.9 16.9 1.0

Reference:

Y.Wine, N.Cohen-Hadar, A.Freeman, F.Frolow. Elucidation of the Mechanism and End Products of Glutaraldehyde Crosslinking Reaction By X-Ray Structure Analysis Biotechnol.Bioeng. V. 98 711 2007.
ISSN: ISSN 0006-3592
PubMed: 17461426
DOI: 10.1002/BIT.21459
Page generated: Sat Dec 12 09:07:46 2020

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