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Sodium in PDB 1y34: Crystal Structure of the Complex of Subtilisin Bpn' with Chymotrypsin Inhibitor 2 E60A Mutant

Enzymatic activity of Crystal Structure of the Complex of Subtilisin Bpn' with Chymotrypsin Inhibitor 2 E60A Mutant

All present enzymatic activity of Crystal Structure of the Complex of Subtilisin Bpn' with Chymotrypsin Inhibitor 2 E60A Mutant:
3.4.21.62;

Protein crystallography data

The structure of Crystal Structure of the Complex of Subtilisin Bpn' with Chymotrypsin Inhibitor 2 E60A Mutant, PDB code: 1y34 was solved by E.S.Radisky, C.J.Lu, G.Kwan, 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 / 1.55
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 93.820, 93.820, 185.332, 90.00, 90.00, 120.00
R / Rfree (%) 15.5 / 18

Other elements in 1y34:

The structure of Crystal Structure of the Complex of Subtilisin Bpn' with Chymotrypsin Inhibitor 2 E60A 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 E60A Mutant (pdb code 1y34). 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 E60A Mutant, PDB code: 1y34:

Sodium binding site 1 out of 1 in 1y34

Go back to Sodium Binding Sites List in 1y34
Sodium binding site 1 out of 1 in the Crystal Structure of the Complex of Subtilisin Bpn' with Chymotrypsin Inhibitor 2 E60A 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 E60A Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Na1002

b:15.0
occ:1.00
 O E:VAL174 2.3 12.6 1.0
O E:TYR171 2.3 13.5 1.0
O E:HOH5137 2.4 18.0 1.0
O E:GLY169 2.4 12.6 1.0
O E:HOH5036 2.4 15.1 1.0
C E:TYR171 3.3 14.7 1.0
C E:VAL174 3.4 11.9 1.0
C E:GLY169 3.6 13.3 1.0
C E:LYS170 3.9 14.2 1.0
N E:TYR171 3.9 14.2 1.0
CA E:PRO172 4.0 13.5 1.0
N E:PRO172 4.0 13.7 1.0
N E:ALA176 4.1 10.1 1.0
N E:VAL174 4.1 11.3 1.0
O E:LYS170 4.1 15.4 1.0
CB E:ALA176 4.1 10.8 1.0
CA E:VAL174 4.1 10.8 1.0
O E:GLU195 4.2 15.7 1.0
C E:PRO172 4.2 12.6 1.0
O E:PRO172 4.2 13.7 1.0
CB E:VAL174 4.3 12.5 1.0
CA E:TYR171 4.3 13.1 1.0
CA E:LYS170 4.3 14.8 1.0
N E:LYS170 4.4 12.9 1.0
N E:ILE175 4.5 10.1 1.0
O E:HOH5093 4.5 22.6 1.0
O E:HOH5251 4.6 34.3 1.0
CA E:GLY169 4.6 10.9 1.0
O E:HOH5384 4.7 44.0 1.0
CA E:ILE175 4.7 10.6 1.0
C E:ILE175 4.7 11.1 1.0
CA E:ALA176 4.7 10.9 1.0
NH2 E:ARG247 4.7 17.1 1.0
CG1 E:VAL174 4.9 11.8 1.0
N E:SER173 4.9 13.0 1.0
O E:PRO168 4.9 11.4 1.0
CB E:GLU195 4.9 15.6 1.0

Reference:

E.S.Radisky, C.J.Lu, G.Kwan, D.E.Koshland Jr.. Role of the Intramolecular Hydrogen Bond Network in the Inhibitory Power of Chymotrypsin Inhibitor 2 Biochemistry V. 44 6823 2005.
ISSN: ISSN 0006-2960
PubMed: 15865427
DOI: 10.1021/BI047301W
Page generated: Mon Oct 7 00:36:33 2024

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