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Sodium in PDB 3a96: Crystal Structure of Hen Egg White Lysozyme Soaked with 100MM RHCL3 at PH2.2

Enzymatic activity of Crystal Structure of Hen Egg White Lysozyme Soaked with 100MM RHCL3 at PH2.2

All present enzymatic activity of Crystal Structure of Hen Egg White Lysozyme Soaked with 100MM RHCL3 at PH2.2:
3.2.1.17;

Protein crystallography data

The structure of Crystal Structure of Hen Egg White Lysozyme Soaked with 100MM RHCL3 at PH2.2, PDB code: 3a96 was solved by S.Abe, T.Koshiyama, T.Ohki, T.Hikage, Y.Watanabe, T.Ueno, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 18.38 / 1.75
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 77.967, 77.967, 37.140, 90.00, 90.00, 90.00
R / Rfree (%) 19.4 / 22.5

Other elements in 3a96:

The structure of Crystal Structure of Hen Egg White Lysozyme Soaked with 100MM RHCL3 at PH2.2 also contains other interesting chemical elements:

Rhodium (Rh) 4 atoms
Chlorine (Cl) 4 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of Hen Egg White Lysozyme Soaked with 100MM RHCL3 at PH2.2 (pdb code 3a96). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Crystal Structure of Hen Egg White Lysozyme Soaked with 100MM RHCL3 at PH2.2, PDB code: 3a96:

Sodium binding site 1 out of 1 in 3a96

Go back to Sodium Binding Sites List in 3a96
Sodium binding site 1 out of 1 in the Crystal Structure of Hen Egg White Lysozyme Soaked with 100MM RHCL3 at PH2.2


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of Hen Egg White Lysozyme Soaked with 100MM RHCL3 at PH2.2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na130

b:21.3
occ:1.00
 O A:SER60 2.3 17.3 1.0
O A:HOH191 2.3 18.2 1.0
O A:HOH140 2.5 15.8 1.0
O A:ARG73 2.5 19.5 1.0
OG A:SER72 2.5 23.9 1.0
O A:CYS64 2.6 14.8 1.0
CB A:SER72 3.2 22.7 1.0
C A:SER60 3.5 16.3 1.0
C A:ARG73 3.5 19.8 1.0
C A:CYS64 3.6 15.0 1.0
N A:ARG73 3.9 21.4 1.0
CA A:ASN65 3.9 15.0 1.0
CA A:SER60 4.1 15.0 1.0
C A:SER72 4.1 22.7 1.0
N A:ASN65 4.2 13.9 1.0
CB A:SER60 4.3 14.8 1.0
CA A:ARG73 4.3 20.8 1.0
CA A:SER72 4.3 23.4 1.0
N A:ASN74 4.4 18.4 1.0
O A:HOH193 4.5 34.6 1.0
N A:ARG61 4.5 16.9 1.0
N A:CYS64 4.6 15.4 1.0
C A:ARG61 4.6 18.3 1.0
ND2 A:ASN65 4.6 14.5 1.0
CA A:ASN74 4.6 17.6 1.0
N A:ASP66 4.6 13.8 1.0
CL A:CL132 4.6 23.0 1.0
CB A:THR69 4.6 17.2 1.0
O A:ARG61 4.7 19.0 1.0
O A:SER72 4.7 22.8 1.0
CA A:ARG61 4.7 18.1 0.5
CA A:CYS64 4.7 15.0 1.0
CB A:ASN74 4.8 17.9 1.0
CB A:ASN65 4.8 15.5 1.0
C A:ASN65 4.8 13.8 1.0
CA A:ARG61 4.8 17.7 0.5
N A:TRP62 4.9 18.2 1.0
O A:THR69 4.9 18.2 1.0

Reference:

T.Ueno, S.Abe, T.Koshiyama, T.Ohki, T.Hikage, Y.Watanabe. Elucidation of Metal-Ion Accumulation Induced By Hydrogen Bonds on Protein Surfaces By Using Porous Lysozyme Crystals Containing Rh(III) Ions As the Model Surfaces Chemistry V. 16 2730 2010.
ISSN: ISSN 0947-6539
PubMed: 20146274
DOI: 10.1002/CHEM.200903269
Page generated: Mon Oct 7 05:45:55 2024

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