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Sodium in PDB 1tm3: Crystal Structure of the Complex of Subtilisin Bpn' with Chymotrypsin Inhibitor 2 M59K Mutant

Enzymatic activity of Crystal Structure of the Complex of Subtilisin Bpn' with Chymotrypsin Inhibitor 2 M59K Mutant

All present enzymatic activity of Crystal Structure of the Complex of Subtilisin Bpn' with Chymotrypsin Inhibitor 2 M59K Mutant:
3.4.21.62;

Protein crystallography data

The structure of Crystal Structure of the Complex of Subtilisin Bpn' with Chymotrypsin Inhibitor 2 M59K Mutant, PDB code: 1tm3 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 / 1.57
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 94.200, 94.200, 187.624, 90.00, 90.00, 120.00
R / Rfree (%) 16.6 / 18.4

Other elements in 1tm3:

The structure of Crystal Structure of the Complex of Subtilisin Bpn' with Chymotrypsin Inhibitor 2 M59K 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 M59K Mutant (pdb code 1tm3). 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 M59K Mutant, PDB code: 1tm3:

Sodium binding site 1 out of 1 in 1tm3

Go back to Sodium Binding Sites List in 1tm3
Sodium binding site 1 out of 1 in the Crystal Structure of the Complex of Subtilisin Bpn' with Chymotrypsin Inhibitor 2 M59K 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 M59K Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Na451

b:16.0
occ:1.00
O E:VAL174 2.3 12.9 1.0
O E:TYR171 2.3 15.8 1.0
O E:HOH592 2.4 20.9 1.0
O E:GLY169 2.4 14.2 1.0
O E:HOH488 2.5 15.8 1.0
C E:TYR171 3.3 16.1 1.0
C E:VAL174 3.4 12.1 1.0
C E:GLY169 3.6 14.8 1.0
C E:LYS170 3.9 16.4 1.0
N E:TYR171 4.0 15.4 1.0
N E:VAL174 4.0 12.8 1.0
CA E:PRO172 4.0 15.9 1.0
N E:PRO172 4.1 15.2 1.0
N E:ALA176 4.1 11.8 1.0
O E:LYS170 4.1 16.8 1.0
CA E:VAL174 4.1 12.4 1.0
C E:PRO172 4.2 15.3 1.0
O E:PRO172 4.2 15.5 1.0
CB E:ALA176 4.2 11.9 1.0
O E:GLU195 4.2 17.8 1.0
CB E:VAL174 4.2 12.0 1.0
CA E:TYR171 4.3 15.8 1.0
O E:HOH758 4.3 45.1 1.0
CA E:LYS170 4.4 16.4 1.0
N E:LYS170 4.4 15.4 1.0
N E:ILE175 4.4 11.6 1.0
O E:HOH548 4.6 22.8 1.0
CA E:GLY169 4.6 14.1 1.0
CA E:ILE175 4.7 11.8 1.0
C E:ILE175 4.7 11.7 1.0
O E:HOH721 4.7 37.2 1.0
CA E:ALA176 4.8 11.1 1.0
NH2 E:ARG247 4.8 17.9 1.0
N E:SER173 4.8 15.1 1.0
CG1 E:VAL174 4.9 13.5 1.0
O E:PRO168 4.9 13.9 1.0
CB E:GLU195 5.0 18.2 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 05:36:32 2020

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