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Sodium in PDB 1tm1: Crystal Structure of the Complex of Subtilisin Bpn' with Chymotrypsin Inhibitor 2

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

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

Protein crystallography data

The structure of Crystal Structure of the Complex of Subtilisin Bpn' with Chymotrypsin Inhibitor 2, PDB code: 1tm1 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 / 1.70
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 93.720, 93.720, 185.853, 90.00, 90.00, 120.00
R / Rfree (%) 15.1 / 18.2

Other elements in 1tm1:

The structure of Crystal Structure of the Complex of Subtilisin Bpn' with Chymotrypsin Inhibitor 2 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 (pdb code 1tm1). 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, PDB code: 1tm1:

Sodium binding site 1 out of 1 in 1tm1

Go back to Sodium Binding Sites List in 1tm1
Sodium binding site 1 out of 1 in the Crystal Structure of the Complex of Subtilisin Bpn' with Chymotrypsin Inhibitor 2


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 within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Na521

b:16.3
occ:1.00
 O E:VAL174 2.3 13.9 1.0
O E:TYR171 2.3 17.3 1.0
O E:HOH664 2.3 20.2 1.0
O E:GLY169 2.4 14.9 1.0
O E:HOH560 2.5 15.8 1.0
C E:TYR171 3.3 17.6 1.0
C E:VAL174 3.4 13.3 1.0
C E:GLY169 3.6 14.9 1.0
C E:LYS170 3.9 16.7 1.0
N E:TYR171 4.0 16.5 1.0
N E:PRO172 4.0 16.6 1.0
O E:LYS170 4.0 17.7 1.0
CA E:PRO172 4.0 16.0 1.0
N E:VAL174 4.1 12.7 1.0
N E:ALA176 4.1 11.2 1.0
CB E:ALA176 4.1 12.1 1.0
CA E:VAL174 4.1 13.0 1.0
O E:GLU195 4.2 18.1 1.0
C E:PRO172 4.2 15.5 1.0
O E:PRO172 4.2 14.7 1.0
CB E:VAL174 4.2 13.2 1.0
CA E:TYR171 4.2 16.1 1.0
CA E:LYS170 4.3 16.2 1.0
N E:LYS170 4.4 14.8 1.0
N E:ILE175 4.5 11.9 1.0
CA E:GLY169 4.6 13.2 1.0
O E:HOH619 4.6 23.1 1.0
O E:HOH778 4.6 37.4 1.0
CA E:ILE175 4.7 11.0 1.0
C E:ILE175 4.7 11.9 1.0
CA E:ALA176 4.7 11.7 1.0
NH2 E:ARG247 4.7 16.4 1.0
O E:PRO168 4.8 13.1 1.0
N E:SER173 4.9 15.0 1.0
CB E:GLU195 4.9 18.5 1.0
CG1 E:VAL174 4.9 12.6 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: Sun Aug 17 07:52:44 2025

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