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Sodium in PDB 2w1q: Unique Ligand Binding Specificity For A Family 32 Carbohydrate- Binding Module From the Mu Toxin Produced By Clostridium Perfringens

Enzymatic activity of Unique Ligand Binding Specificity For A Family 32 Carbohydrate- Binding Module From the Mu Toxin Produced By Clostridium Perfringens

All present enzymatic activity of Unique Ligand Binding Specificity For A Family 32 Carbohydrate- Binding Module From the Mu Toxin Produced By Clostridium Perfringens:
3.2.1.35;

Protein crystallography data

The structure of Unique Ligand Binding Specificity For A Family 32 Carbohydrate- Binding Module From the Mu Toxin Produced By Clostridium Perfringens, PDB code: 2w1q was solved by E.Ficko-Blean, A.B.Boraston, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.39 / 1.60
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 56.118, 61.470, 82.950, 90.00, 90.00, 90.00
R / Rfree (%) 14.9 / 19.9

Other elements in 2w1q:

The structure of Unique Ligand Binding Specificity For A Family 32 Carbohydrate- Binding Module From the Mu Toxin Produced By Clostridium Perfringens also contains other interesting chemical elements:

Calcium (Ca) 2 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Unique Ligand Binding Specificity For A Family 32 Carbohydrate- Binding Module From the Mu Toxin Produced By Clostridium Perfringens (pdb code 2w1q). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Unique Ligand Binding Specificity For A Family 32 Carbohydrate- Binding Module From the Mu Toxin Produced By Clostridium Perfringens, PDB code: 2w1q:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in 2w1q

Go back to Sodium Binding Sites List in 2w1q
Sodium binding site 1 out of 2 in the Unique Ligand Binding Specificity For A Family 32 Carbohydrate- Binding Module From the Mu Toxin Produced By Clostridium Perfringens


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Unique Ligand Binding Specificity For A Family 32 Carbohydrate- Binding Module From the Mu Toxin Produced By Clostridium Perfringens within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na1948

b:13.5
occ:1.00
O A:HOH2034 2.9 33.5 1.0
NZ A:LYS908 3.1 21.0 1.0
N A:LYS908 3.4 13.0 1.0
OD1 A:ASN871 3.4 20.0 1.0
O A:HOH2005 3.5 23.6 1.0
CA A:ASN871 3.6 12.4 1.0
CG A:LYS908 3.7 15.0 1.0
CB A:ASN871 3.7 13.5 1.0
N A:ASN871 3.7 11.7 1.0
CA A:GLY907 3.8 14.2 1.0
CG A:ASN871 4.0 15.5 1.0
CE A:LYS908 4.0 21.6 1.0
C A:LYS870 4.1 11.3 1.0
CB A:LYS908 4.1 13.7 1.0
C A:GLY907 4.1 13.5 1.0
O A:LYS870 4.2 11.7 1.0
CA A:LYS908 4.3 13.3 1.0
CD A:LYS908 4.4 18.4 1.0
O A:HOH2004 4.5 34.9 1.0
O A:HOH2184 4.6 19.0 1.0
O A:HOH2185 4.6 31.4 1.0
O A:HOH2129 4.8 17.1 1.0
CA A:LYS870 4.9 11.2 1.0
C A:ASN871 5.0 12.2 1.0

Sodium binding site 2 out of 2 in 2w1q

Go back to Sodium Binding Sites List in 2w1q
Sodium binding site 2 out of 2 in the Unique Ligand Binding Specificity For A Family 32 Carbohydrate- Binding Module From the Mu Toxin Produced By Clostridium Perfringens


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of Unique Ligand Binding Specificity For A Family 32 Carbohydrate- Binding Module From the Mu Toxin Produced By Clostridium Perfringens within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Na1947

b:16.1
occ:1.00
O B:HOH2048 3.2 13.2 1.0
N B:GLU814 3.4 11.1 1.0
O B:HOH2030 3.6 28.8 1.0
O B:HOH2053 3.6 23.5 1.0
CB B:GLU814 4.0 13.0 1.0
CA B:SER813 4.0 10.9 1.0
CE1 B:PHE850 4.0 13.5 1.0
CZ B:PHE850 4.2 13.3 1.0
C B:SER813 4.2 10.9 1.0
CA B:GLU814 4.3 11.9 1.0
CB B:SER813 4.7 9.9 1.0
O B:HOH2104 4.7 20.5 1.0
O B:ARG812 4.8 11.0 1.0
OG B:SER813 4.8 10.1 1.0
N B:SER813 5.0 10.8 1.0

Reference:

E.Ficko-Blean, A.B.Boraston. N-Acetylglucosamine Recognition By A Family 32 Carbohydrate-Binding Module From Clostridium Perfringens Nagh. J.Mol.Biol. V. 390 208 2009.
ISSN: ISSN 0022-2836
PubMed: 19422833
DOI: 10.1016/J.JMB.2009.04.066
Page generated: Tue Dec 15 05:57:04 2020

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