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Sodium in PDB 1to1: Crystal Structure of the Complex of Subtilisin Bpn' with Chymotrypsin Inhibitor 2 Y61A Mutant

Enzymatic activity of Crystal Structure of the Complex of Subtilisin Bpn' with Chymotrypsin Inhibitor 2 Y61A Mutant

All present enzymatic activity of Crystal Structure of the Complex of Subtilisin Bpn' with Chymotrypsin Inhibitor 2 Y61A Mutant:
3.4.21.62;

Protein crystallography data

The structure of Crystal Structure of the Complex of Subtilisin Bpn' with Chymotrypsin Inhibitor 2 Y61A Mutant, PDB code: 1to1 was solved by E.S.Radisky, G.Kwan, C.J.Karen Lu, D.E.Koshland Jr., with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 81.65 / 1.68
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 94.087, 94.087, 185.769, 90.00, 90.00, 120.00
R / Rfree (%) 15.6 / 18.2

Other elements in 1to1:

The structure of Crystal Structure of the Complex of Subtilisin Bpn' with Chymotrypsin Inhibitor 2 Y61A Mutant also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of the Complex of Subtilisin Bpn' with Chymotrypsin Inhibitor 2 Y61A Mutant (pdb code 1to1). 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 the Complex of Subtilisin Bpn' with Chymotrypsin Inhibitor 2 Y61A Mutant, PDB code: 1to1:

Sodium binding site 1 out of 1 in 1to1

Go back to Sodium Binding Sites List in 1to1
Sodium binding site 1 out of 1 in the Crystal Structure of the Complex of Subtilisin Bpn' with Chymotrypsin Inhibitor 2 Y61A Mutant


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 the Complex of Subtilisin Bpn' with Chymotrypsin Inhibitor 2 Y61A Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Na511

b:18.1
occ:1.00
O E:VAL174 2.3 13.7 1.0
O E:TYR171 2.4 15.5 1.0
O E:HOH651 2.4 21.7 1.0
O E:HOH549 2.4 17.9 1.0
O E:GLY169 2.4 15.1 1.0
C E:TYR171 3.3 17.7 1.0
C E:VAL174 3.4 14.7 1.0
C E:GLY169 3.6 16.4 1.0
C E:LYS170 3.9 17.0 1.0
N E:ALA176 4.0 11.2 1.0
N E:TYR171 4.0 16.5 1.0
N E:PRO172 4.0 16.7 1.0
CA E:PRO172 4.1 17.1 1.0
N E:VAL174 4.1 13.9 1.0
O E:LYS170 4.1 16.9 1.0
O E:GLU195 4.1 17.5 1.0
CB E:ALA176 4.1 12.1 1.0
CA E:VAL174 4.1 13.8 1.0
C E:PRO172 4.2 16.8 1.0
O E:PRO172 4.2 17.3 1.0
CB E:VAL174 4.3 14.1 1.0
CA E:TYR171 4.3 16.6 1.0
CA E:LYS170 4.4 16.5 1.0
O E:HOH607 4.4 25.3 1.0
N E:LYS170 4.4 16.1 1.0
N E:ILE175 4.5 12.5 1.0
O E:HOH765 4.5 38.7 1.0
CA E:GLY169 4.6 14.3 1.0
C E:ILE175 4.6 12.5 1.0
CA E:ILE175 4.6 12.6 1.0
CA E:ALA176 4.7 11.9 1.0
NH2 E:ARG247 4.7 17.2 1.0
N E:SER173 4.9 16.0 1.0
CB E:GLU195 4.9 17.8 1.0
CG1 E:VAL174 4.9 13.8 1.0
O E:PRO168 5.0 14.6 1.0

Reference:

E.S.Radisky, G.Kwan, C.J.Karen Lu, D.E.Koshland Jr.. Binding, Proteolytic, and Crystallographic Analyses of Mutations at the Protease-Inhibitor Interface of the Subtilisin Bpn'/Chymotrypsin Inhibitor 2 Complex(,). Biochemistry V. 43 13648 2004.
ISSN: ISSN 0006-2960
PubMed: 15504027
DOI: 10.1021/BI048797K
Page generated: Tue Dec 15 05:36:36 2020

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