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Sodium in PDB 3unx: Bond Length Analysis of Asp, Glu and His Residues in Subtilisin Carlsberg at 1.26A Resolution

Enzymatic activity of Bond Length Analysis of Asp, Glu and His Residues in Subtilisin Carlsberg at 1.26A Resolution

All present enzymatic activity of Bond Length Analysis of Asp, Glu and His Residues in Subtilisin Carlsberg at 1.26A Resolution:
3.4.21.62;

Protein crystallography data

The structure of Bond Length Analysis of Asp, Glu and His Residues in Subtilisin Carlsberg at 1.26A Resolution, PDB code: 3unx was solved by S.J.Fisher, J.R.Helliwell, M.P.Blakeley, M.Cianci, S.Mcsweeny, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 13.79 / 1.26
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 52.099, 55.159, 75.453, 90.00, 90.00, 90.00
R / Rfree (%) 11.8 / 13.9

Other elements in 3unx:

The structure of Bond Length Analysis of Asp, Glu and His Residues in Subtilisin Carlsberg at 1.26A Resolution also contains other interesting chemical elements:

Calcium (Ca) 2 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Bond Length Analysis of Asp, Glu and His Residues in Subtilisin Carlsberg at 1.26A Resolution (pdb code 3unx). 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 Bond Length Analysis of Asp, Glu and His Residues in Subtilisin Carlsberg at 1.26A Resolution, PDB code: 3unx:

Sodium binding site 1 out of 1 in 3unx

Go back to Sodium Binding Sites List in 3unx
Sodium binding site 1 out of 1 in the Bond Length Analysis of Asp, Glu and His Residues in Subtilisin Carlsberg at 1.26A Resolution


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Bond Length Analysis of Asp, Glu and His Residues in Subtilisin Carlsberg at 1.26A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na281

b:6.8
occ:1.00
 O A:VAL174 2.3 6.5 1.0
O A:ALA169 2.3 7.3 1.0
O A:HOH519 2.3 11.4 1.0
O A:TYR171 2.4 8.1 1.0
O A:HOH517 2.4 7.8 1.0
C A:TYR171 3.3 8.2 1.0
C A:VAL174 3.4 5.9 1.0
HB A:VAL174 3.4 7.7 1.0
H A:VAL174 3.5 7.8 1.0
HB2 A:ALA176 3.5 7.7 1.0
C A:ALA169 3.5 7.4 1.0
H A:ALA176 3.6 6.6 1.0
HA A:ASP172 3.6 12.5 1.0
HB3 A:GLU195 3.7 12.0 1.0
C A:LYS170 3.8 8.7 1.0
HO2 A:GOL279 3.9 41.0 1.0
HA A:LYS170 3.9 10.0 1.0
N A:TYR171 3.9 7.7 1.0
O A:LYS170 3.9 9.5 1.0
N A:ALA176 4.0 5.5 1.0
HH22 A:ARG247 4.1 13.4 1.0
CA A:VAL174 4.1 5.9 1.0
N A:VAL174 4.1 6.5 1.0
N A:ASP172 4.1 9.4 1.0
CB A:VAL174 4.2 6.4 1.0
HA A:ILE175 4.2 6.7 1.0
CA A:ASP172 4.2 10.4 1.0
H11 A:GOL279 4.2 40.7 1.0
CA A:LYS170 4.2 8.3 1.0
H A:TYR171 4.2 9.2 1.0
CB A:ALA176 4.2 6.5 1.0
HB3 A:ALA176 4.2 7.7 1.0
CA A:TYR171 4.3 8.5 1.0
HA A:ALA169 4.3 8.2 1.0
N A:LYS170 4.3 7.4 1.0
HH21 A:ARG247 4.3 13.4 1.0
O A:GLU195 4.4 8.3 1.0
N A:ILE175 4.4 5.5 1.0
C A:ASP172 4.4 8.9 1.0
NH2 A:ARG247 4.5 11.2 1.0
HG12 A:VAL174 4.5 8.3 1.0
OE1 A:GLU197 4.5 10.4 1.0
CA A:ALA169 4.5 6.8 1.0
O1 A:GOL279 4.6 34.6 1.0
C A:ILE175 4.6 5.8 1.0
CA A:ILE175 4.6 5.6 1.0
O A:ASP172 4.6 10.1 1.0
HO1 A:GOL279 4.7 41.6 1.0
CB A:GLU195 4.7 10.0 1.0
CA A:ALA176 4.7 5.8 1.0
O2 A:GOL279 4.8 34.2 1.0
HG2 A:GLU195 4.8 14.4 1.0
O A:PRO168 4.9 7.8 1.0
C1 A:GOL279 4.9 34.0 1.0
CG1 A:VAL174 4.9 6.9 1.0
HB1 A:ALA169 4.9 8.8 1.0
HA A:TYR171 4.9 10.2 1.0
HB2 A:TYR171 4.9 11.0 1.0
H A:ASP172 4.9 11.3 1.0
HA A:ALA176 5.0 6.9 1.0

Reference:

S.J.Fisher, M.P.Blakeley, M.Cianci, S.Mcsweeney, J.R.Helliwell. Protonation-State Determination in Proteins Using High-Resolution X-Ray Crystallography: Effects of Resolution and Completeness. Acta Crystallogr.,Sect.D V. 68 800 2012.
ISSN: ISSN 0907-4449
PubMed: 22751665
DOI: 10.1107/S0907444912012589
Page generated: Mon Oct 7 13:29:26 2024

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