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Sodium in PDB 5ffn: Complex of Subtilase Subty From Bacillus Sp. TY145 with Chymotrypsin Inhibitor CI2A

Enzymatic activity of Complex of Subtilase Subty From Bacillus Sp. TY145 with Chymotrypsin Inhibitor CI2A

All present enzymatic activity of Complex of Subtilase Subty From Bacillus Sp. TY145 with Chymotrypsin Inhibitor CI2A:
3.4.21.14;

Protein crystallography data

The structure of Complex of Subtilase Subty From Bacillus Sp. TY145 with Chymotrypsin Inhibitor CI2A, PDB code: 5ffn was solved by K.E.Mcauley, A.Svendsen, P.R.Oestergaard, J.Dohnalek, K.S.Wilson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.00 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 58.753, 66.838, 107.082, 90.00, 90.00, 90.00
R / Rfree (%) 15.1 / 18.8

Other elements in 5ffn:

The structure of Complex of Subtilase Subty From Bacillus Sp. TY145 with Chymotrypsin Inhibitor CI2A also contains other interesting chemical elements:

Calcium (Ca) 2 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Complex of Subtilase Subty From Bacillus Sp. TY145 with Chymotrypsin Inhibitor CI2A (pdb code 5ffn). 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 Complex of Subtilase Subty From Bacillus Sp. TY145 with Chymotrypsin Inhibitor CI2A, PDB code: 5ffn:

Sodium binding site 1 out of 1 in 5ffn

Go back to Sodium Binding Sites List in 5ffn
Sodium binding site 1 out of 1 in the Complex of Subtilase Subty From Bacillus Sp. TY145 with Chymotrypsin Inhibitor CI2A


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Complex of Subtilase Subty From Bacillus Sp. TY145 with Chymotrypsin Inhibitor CI2A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na403

b:10.2
occ:1.00
 O A:LEU184 2.3 10.2 1.0
O A:HOH630 2.3 10.1 1.0
O A:GLY182 2.3 10.8 1.0
O A:ALA187 2.4 10.8 1.0
O A:HOH692 2.4 8.3 1.0
C A:LEU184 3.4 10.4 1.0
C A:ALA187 3.5 10.7 1.0
C A:GLY182 3.5 11.0 1.0
N A:LEU184 3.6 10.9 1.0
C A:GLY183 3.6 11.0 1.0
N A:ALA189 3.9 9.1 1.0
CA A:GLY183 3.9 11.1 1.0
O A:ASP225 4.0 10.3 1.0
CB A:ALA189 4.0 10.1 1.0
O A:GLY183 4.1 10.4 1.0
CA A:LEU184 4.1 11.3 1.0
N A:GLY183 4.1 10.2 1.0
N A:ALA187 4.2 10.6 1.0
CA A:ALA187 4.2 11.0 1.0
N A:VAL185 4.4 10.9 1.0
CB A:ALA187 4.4 11.1 1.0
N A:VAL188 4.5 9.8 1.0
CG2 A:ILE221 4.5 14.1 1.0
CA A:VAL185 4.5 11.3 1.0
CA A:ALA189 4.5 9.1 1.0
OE1 A:GLU227 4.5 8.5 1.0
C A:VAL185 4.5 10.6 1.0
C A:VAL188 4.6 9.7 1.0
O A:VAL185 4.6 11.5 1.0
CA A:VAL188 4.6 9.5 1.0
CA A:GLY182 4.7 11.1 1.0
O A:PRO181 4.8 9.3 1.0
NH2 A:ARG277 4.8 13.2 1.0
CB A:LEU184 5.0 10.5 1.0

Reference:

J.Dohnalek, K.E.Mcauley, A.M.Brzozowski, P.R.Oestergaard, A.Svendsen, K.S.Wilson. Stabilization of Enzymes By Metal Binding: Structures of Two Alkalophilic Bacillus Subtilases and Analysis of the Second Metal-Binding Site of the Subtilase Family To Be Published 203 2016.
DOI: 10.4032/9789814669337
Page generated: Mon Oct 7 21:01:04 2024

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