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Potassium in PDB 3s27: The Crystal Structure of Sucrose Synthase-1 From Arabidopsis Thaliana and Its Functional Implications.

Enzymatic activity of The Crystal Structure of Sucrose Synthase-1 From Arabidopsis Thaliana and Its Functional Implications.

All present enzymatic activity of The Crystal Structure of Sucrose Synthase-1 From Arabidopsis Thaliana and Its Functional Implications.:
2.4.1.13;

Protein crystallography data

The structure of The Crystal Structure of Sucrose Synthase-1 From Arabidopsis Thaliana and Its Functional Implications., PDB code: 3s27 was solved by Y.Zheng, R.M.Garavito, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.00 / 2.91
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 276.212, 263.704, 159.663, 90.00, 108.80, 90.00
R / Rfree (%) 18.6 / 23.7

Potassium Binding Sites:

The binding sites of Potassium atom in the The Crystal Structure of Sucrose Synthase-1 From Arabidopsis Thaliana and Its Functional Implications. (pdb code 3s27). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 8 binding sites of Potassium where determined in the The Crystal Structure of Sucrose Synthase-1 From Arabidopsis Thaliana and Its Functional Implications., PDB code: 3s27:
Jump to Potassium binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Potassium binding site 1 out of 8 in 3s27

Go back to Potassium Binding Sites List in 3s27
Potassium binding site 1 out of 8 in the The Crystal Structure of Sucrose Synthase-1 From Arabidopsis Thaliana and Its Functional Implications.


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of The Crystal Structure of Sucrose Synthase-1 From Arabidopsis Thaliana and Its Functional Implications. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K931

b:61.3
occ:1.00
 O A:LEU194 2.5 43.7 1.0
O A:LEU184 2.5 41.3 1.0
O A:LEU196 2.6 50.5 1.0
O A:ARG185 2.7 46.0 1.0
OD1 A:ASN193 2.8 41.8 1.0
O A:HIS187 2.8 40.8 1.0
C A:ARG185 3.1 45.9 1.0
CA A:ARG185 3.4 45.0 1.0
N A:HIS187 3.5 41.7 1.0
C A:LEU184 3.5 41.2 1.0
C A:LEU194 3.6 42.5 1.0
N A:LEU194 3.7 38.1 1.0
C A:HIS187 3.7 43.8 1.0
CG A:ASN193 3.8 47.8 1.0
C A:LEU196 3.8 44.6 1.0
N A:LEU186 3.9 45.9 1.0
N A:ARG185 3.9 41.4 1.0
CA A:HIS187 4.0 42.3 1.0
C A:LEU186 4.1 44.8 1.0
N A:LEU196 4.1 39.5 1.0
CA A:LEU194 4.2 38.6 1.0
CB A:HIS187 4.2 41.8 1.0
CA A:LEU186 4.4 46.6 1.0
CA A:LEU196 4.5 38.0 1.0
ND2 A:ASN193 4.5 51.0 1.0
C A:ASN193 4.7 40.1 1.0
C A:MSE195 4.7 37.8 1.0
N A:MSE195 4.7 40.2 1.0
CB A:ASN193 4.7 45.9 1.0
CA A:ASN193 4.8 41.5 1.0
O A:LEU186 4.8 43.8 1.0
CB A:MSE195 4.8 42.0 1.0
N A:SER197 4.8 43.3 1.0
CB A:ARG185 4.8 52.3 1.0
CA A:LEU184 4.8 41.1 1.0
CB A:LEU194 4.9 38.6 1.0
N A:SER188 4.9 42.6 1.0
CA A:MSE195 4.9 42.2 1.0
CA A:SER197 5.0 43.8 1.0

Potassium binding site 2 out of 8 in 3s27

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Potassium binding site 2 out of 8 in the The Crystal Structure of Sucrose Synthase-1 From Arabidopsis Thaliana and Its Functional Implications.


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of The Crystal Structure of Sucrose Synthase-1 From Arabidopsis Thaliana and Its Functional Implications. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K931

b:75.0
occ:1.00
 O B:LEU196 2.5 57.5 1.0
O B:HIS187 2.6 54.2 1.0
O B:LEU194 2.7 49.4 1.0
O B:ARG185 2.7 56.3 1.0
OD1 B:ASN193 2.8 53.9 1.0
CG B:ASN193 3.3 59.0 1.0
O B:LEU184 3.4 53.5 1.0
C B:ARG185 3.4 55.0 1.0
ND2 B:ASN193 3.6 63.6 1.0
C B:HIS187 3.6 56.2 1.0
N B:LEU194 3.6 50.2 1.0
C B:LEU196 3.7 52.6 1.0
N B:HIS187 3.7 55.4 1.0
C B:LEU194 3.8 49.4 1.0
C B:LEU186 3.9 56.1 1.0
CA B:ARG185 4.0 56.8 1.0
CA B:HIS187 4.1 56.6 1.0
N B:LEU186 4.2 54.5 1.0
O B:LEU186 4.2 51.6 1.0
N B:LEU196 4.3 50.7 1.0
C B:LEU184 4.3 54.4 1.0
CA B:LEU194 4.3 49.5 1.0
CB B:ASN193 4.3 58.1 1.0
C B:ASN193 4.4 51.6 1.0
CA B:ASN193 4.5 54.8 1.0
CB B:HIS187 4.5 49.0 1.0
CA B:LEU186 4.5 58.0 1.0
CA B:LEU196 4.5 49.6 1.0
N B:ARG185 4.6 56.2 1.0
N B:SER197 4.6 56.3 1.0
CA B:SER197 4.7 58.5 1.0
N B:SER188 4.7 59.9 1.0
C B:MSE195 4.9 46.7 1.0
N B:MSE195 4.9 44.3 1.0

Potassium binding site 3 out of 8 in 3s27

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Potassium binding site 3 out of 8 in the The Crystal Structure of Sucrose Synthase-1 From Arabidopsis Thaliana and Its Functional Implications.


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of The Crystal Structure of Sucrose Synthase-1 From Arabidopsis Thaliana and Its Functional Implications. within 5.0Å range:
probe atom residue distance (Å) B Occ
C:K931

b:69.3
occ:1.00
 O C:LEU196 2.5 49.9 1.0
O C:LEU194 2.5 41.7 1.0
O C:ARG185 2.6 48.9 1.0
O C:HIS187 2.7 51.5 1.0
OD1 C:ASN193 2.8 52.2 1.0
O C:LEU184 2.9 42.9 1.0
C C:ARG185 3.1 47.7 1.0
CG C:ASN193 3.4 53.8 1.0
CA C:ARG185 3.6 45.1 1.0
C C:LEU196 3.6 49.4 1.0
C C:LEU194 3.7 45.5 1.0
ND2 C:ASN193 3.7 53.8 1.0
N C:LEU194 3.8 45.2 1.0
C C:HIS187 3.8 49.0 1.0
N C:HIS187 3.8 43.4 1.0
C C:LEU184 3.9 41.4 1.0
N C:LEU196 3.9 46.6 1.0
N C:LEU186 4.0 44.1 1.0
C C:LEU186 4.0 48.5 1.0
N C:ARG185 4.2 44.0 1.0
CA C:HIS187 4.3 41.0 1.0
CA C:LEU194 4.3 46.0 1.0
CA C:LEU196 4.3 46.6 1.0
O C:LEU186 4.4 51.9 1.0
CA C:LEU186 4.4 45.9 1.0
CB C:MSE195 4.6 42.8 1.0
CB C:HIS187 4.6 38.8 1.0
CB C:ASN193 4.6 47.9 1.0
C C:MSE195 4.7 43.2 1.0
N C:SER197 4.7 52.4 1.0
C C:ASN193 4.7 45.3 1.0
N C:MSE195 4.7 43.2 1.0
CA C:ASN193 4.8 44.6 1.0
CA C:MSE195 4.9 41.3 1.0
CA C:SER197 4.9 50.4 1.0
N C:SER188 4.9 52.3 1.0
CB C:ARG185 4.9 47.9 1.0
CB C:LEU196 5.0 41.9 1.0

Potassium binding site 4 out of 8 in 3s27

Go back to Potassium Binding Sites List in 3s27
Potassium binding site 4 out of 8 in the The Crystal Structure of Sucrose Synthase-1 From Arabidopsis Thaliana and Its Functional Implications.


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 4 of The Crystal Structure of Sucrose Synthase-1 From Arabidopsis Thaliana and Its Functional Implications. within 5.0Å range:
probe atom residue distance (Å) B Occ
D:K931

b:61.9
occ:1.00
 O D:ARG185 2.3 46.1 1.0
O D:LEU194 2.5 40.9 1.0
O D:LEU196 2.5 43.6 1.0
O D:HIS187 2.7 46.7 1.0
O D:LEU184 2.8 42.8 1.0
OD1 D:ASN193 2.8 52.8 1.0
C D:ARG185 3.1 42.6 1.0
CG D:ASN193 3.5 52.4 1.0
CA D:ARG185 3.6 42.8 1.0
C D:LEU194 3.7 43.2 1.0
C D:LEU196 3.7 43.9 1.0
N D:HIS187 3.7 43.7 1.0
C D:HIS187 3.7 44.3 1.0
ND2 D:ASN193 3.8 55.7 1.0
C D:LEU184 3.8 41.2 1.0
N D:LEU194 3.8 40.0 1.0
C D:LEU186 4.0 45.6 1.0
N D:LEU186 4.1 44.9 1.0
N D:LEU196 4.1 41.4 1.0
CA D:HIS187 4.1 41.8 1.0
N D:ARG185 4.2 43.7 1.0
CA D:LEU194 4.3 43.5 1.0
O D:LEU186 4.3 46.7 1.0
CB D:HIS187 4.4 41.9 1.0
CA D:LEU196 4.4 44.0 1.0
CA D:LEU186 4.5 47.2 1.0
CB D:MSE195 4.6 42.9 1.0
C D:MSE195 4.7 42.5 1.0
CB D:ASN193 4.7 51.6 1.0
C D:ASN193 4.7 40.1 1.0
N D:MSE195 4.7 41.2 1.0
N D:SER197 4.7 43.5 1.0
CA D:ASN193 4.9 45.7 1.0
CB D:LEU196 4.9 43.9 1.0
CA D:MSE195 4.9 45.4 1.0
N D:SER188 4.9 43.7 1.0
CA D:SER197 4.9 43.5 1.0
CB D:ARG185 5.0 45.2 1.0

Potassium binding site 5 out of 8 in 3s27

Go back to Potassium Binding Sites List in 3s27
Potassium binding site 5 out of 8 in the The Crystal Structure of Sucrose Synthase-1 From Arabidopsis Thaliana and Its Functional Implications.


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 5 of The Crystal Structure of Sucrose Synthase-1 From Arabidopsis Thaliana and Its Functional Implications. within 5.0Å range:
probe atom residue distance (Å) B Occ
E:K931

b:64.2
occ:1.00
 O E:LEU184 2.3 46.5 1.0
O E:LEU196 2.3 45.1 1.0
O E:ARG185 2.4 48.0 1.0
O E:LEU194 2.5 40.2 1.0
C E:ARG185 2.8 46.2 1.0
CA E:ARG185 3.0 39.3 1.0
C E:LEU184 3.2 41.1 1.0
O E:HIS187 3.3 43.1 1.0
C E:LEU196 3.4 40.5 1.0
ND2 E:ASN193 3.4 45.9 1.0
N E:ARG185 3.5 38.4 1.0
N E:LEU196 3.6 42.0 1.0
C E:LEU194 3.7 44.0 1.0
N E:LEU186 3.8 44.3 1.0
N E:HIS187 3.9 43.4 1.0
CA E:LEU196 4.0 39.2 1.0
CG E:ASN193 4.1 49.3 1.0
C E:LEU186 4.2 45.8 1.0
C E:HIS187 4.2 43.1 1.0
N E:LEU194 4.3 42.0 1.0
OD1 E:ASN193 4.3 52.0 1.0
C E:MSE195 4.3 41.3 1.0
CB E:MSE195 4.3 41.0 1.0
CB E:LEU196 4.4 40.2 1.0
CB E:ARG185 4.4 46.1 1.0
CA E:HIS187 4.4 41.5 1.0
CA E:LEU186 4.5 44.4 1.0
N E:SER197 4.5 47.6 1.0
CB E:HIS187 4.6 37.0 1.0
CA E:LEU184 4.6 38.8 1.0
CA E:LEU194 4.6 40.2 1.0
CA E:MSE195 4.6 41.5 1.0
N E:MSE195 4.6 43.5 1.0
O E:LEU186 4.8 44.9 1.0
CA E:SER197 4.8 49.3 1.0
CG E:ARG185 4.8 56.5 1.0

Potassium binding site 6 out of 8 in 3s27

Go back to Potassium Binding Sites List in 3s27
Potassium binding site 6 out of 8 in the The Crystal Structure of Sucrose Synthase-1 From Arabidopsis Thaliana and Its Functional Implications.


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 6 of The Crystal Structure of Sucrose Synthase-1 From Arabidopsis Thaliana and Its Functional Implications. within 5.0Å range:
probe atom residue distance (Å) B Occ
F:K931

b:69.2
occ:1.00
 O F:HIS187 2.6 54.1 1.0
O F:LEU194 2.6 43.5 1.0
O F:LEU196 2.6 54.3 1.0
O F:ARG185 2.7 56.4 1.0
O F:LEU184 2.7 51.4 1.0
OD1 F:ASN193 2.9 61.9 1.0
C F:ARG185 3.2 53.5 1.0
CG F:ASN193 3.5 54.8 1.0
C F:HIS187 3.5 52.1 1.0
ND2 F:ASN193 3.6 56.9 1.0
N F:HIS187 3.6 54.4 1.0
CA F:ARG185 3.6 50.3 1.0
C F:LEU184 3.7 51.5 1.0
C F:LEU194 3.7 48.6 1.0
C F:LEU196 3.7 50.9 1.0
N F:LEU194 3.8 50.9 1.0
C F:LEU186 3.9 55.0 1.0
CA F:HIS187 4.0 51.5 1.0
N F:LEU186 4.0 50.7 1.0
N F:LEU196 4.1 44.4 1.0
N F:ARG185 4.1 50.2 1.0
CB F:HIS187 4.3 48.7 1.0
CA F:LEU194 4.4 50.3 1.0
O F:LEU186 4.4 55.4 1.0
CA F:LEU196 4.4 45.6 1.0
CA F:LEU186 4.4 52.2 1.0
CB F:ASN193 4.7 48.9 1.0
N F:SER188 4.7 54.9 1.0
C F:MSE195 4.7 45.9 1.0
C F:ASN193 4.7 52.2 1.0
N F:SER197 4.8 52.1 1.0
N F:MSE195 4.8 43.9 1.0
CB F:MSE195 4.8 43.7 1.0
CA F:ASN193 4.8 52.5 1.0
CA F:SER197 5.0 51.1 1.0
CA F:MSE195 5.0 44.5 1.0

Potassium binding site 7 out of 8 in 3s27

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Potassium binding site 7 out of 8 in the The Crystal Structure of Sucrose Synthase-1 From Arabidopsis Thaliana and Its Functional Implications.


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 7 of The Crystal Structure of Sucrose Synthase-1 From Arabidopsis Thaliana and Its Functional Implications. within 5.0Å range:
probe atom residue distance (Å) B Occ
G:K931

b:57.7
occ:1.00
 O G:LEU194 2.3 48.0 1.0
O G:LEU184 2.4 41.2 1.0
O G:LEU196 2.5 48.8 1.0
O G:ARG185 2.5 50.7 1.0
O G:HIS187 2.8 44.9 1.0
C G:ARG185 3.0 44.2 1.0
CA G:ARG185 3.4 40.7 1.0
C G:LEU184 3.5 40.0 1.0
C G:LEU194 3.5 45.5 1.0
OD1 G:ASN193 3.5 51.1 1.0
N G:HIS187 3.5 40.0 1.0
C G:LEU196 3.6 46.3 1.0
N G:LEU196 3.7 43.7 1.0
C G:HIS187 3.7 44.5 1.0
N G:LEU194 3.8 43.7 1.0
CG G:ASN193 3.9 50.2 1.0
ND2 G:ASN193 3.9 54.7 1.0
N G:ARG185 3.9 42.6 1.0
CA G:HIS187 3.9 41.8 1.0
N G:LEU186 4.0 44.1 1.0
C G:LEU186 4.0 44.3 1.0
CB G:HIS187 4.1 40.2 1.0
CA G:LEU196 4.1 43.5 1.0
CA G:LEU194 4.2 43.2 1.0
CB G:MSE195 4.3 42.8 1.0
C G:MSE195 4.3 42.1 1.0
N G:MSE195 4.5 42.1 1.0
CA G:LEU186 4.5 44.2 1.0
CA G:MSE195 4.6 41.4 1.0
O G:LEU186 4.6 47.0 1.0
CB G:LEU196 4.7 42.6 1.0
N G:SER197 4.7 50.4 1.0
CB G:ARG185 4.8 40.8 1.0
CA G:LEU184 4.8 38.5 1.0
C G:ASN193 4.8 44.6 1.0
CB G:LEU194 4.9 42.3 1.0
CB G:ASN193 5.0 48.7 1.0
N G:SER188 5.0 47.6 1.0

Potassium binding site 8 out of 8 in 3s27

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Potassium binding site 8 out of 8 in the The Crystal Structure of Sucrose Synthase-1 From Arabidopsis Thaliana and Its Functional Implications.


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 8 of The Crystal Structure of Sucrose Synthase-1 From Arabidopsis Thaliana and Its Functional Implications. within 5.0Å range:
probe atom residue distance (Å) B Occ
H:K931

b:61.2
occ:1.00
 O H:ARG185 2.5 47.8 1.0
O H:LEU196 2.5 44.2 1.0
O H:LEU194 2.7 36.9 1.0
O H:HIS187 2.7 44.5 1.0
OD1 H:ASN193 2.8 51.4 1.0
C H:ARG185 3.2 46.9 1.0
CG H:ASN193 3.3 44.0 1.0
O H:LEU184 3.4 44.5 1.0
ND2 H:ASN193 3.5 48.5 1.0
C H:LEU196 3.7 42.8 1.0
N H:LEU194 3.7 37.1 1.0
C H:HIS187 3.8 45.0 1.0
C H:LEU194 3.8 40.0 1.0
N H:HIS187 3.8 40.6 1.0
C H:LEU186 3.9 44.6 1.0
CA H:ARG185 3.9 45.9 1.0
N H:LEU186 4.1 47.8 1.0
O H:LEU186 4.2 48.8 1.0
CA H:HIS187 4.3 39.1 1.0
N H:LEU196 4.3 40.4 1.0
CB H:ASN193 4.3 40.1 1.0
C H:LEU184 4.4 45.0 1.0
CA H:LEU194 4.4 39.0 1.0
CA H:LEU186 4.4 45.3 1.0
CA H:ASN193 4.5 37.5 1.0
C H:ASN193 4.6 37.2 1.0
CA H:LEU196 4.6 39.0 1.0
N H:ARG185 4.6 46.6 1.0
N H:SER197 4.6 44.5 1.0
CB H:HIS187 4.7 36.3 1.0
CA H:SER197 4.7 45.9 1.0
N H:SER188 4.9 46.5 1.0
C H:MSE195 4.9 38.0 1.0
N H:MSE195 4.9 39.0 1.0
CB H:MSE195 4.9 41.6 1.0
CG H:GLU239 5.0 42.1 1.0

Reference:

Y.Zheng, S.Anderson, Y.Zhang, R.M.Garavito. The Structure of Sucrose Synthase-1 From Arabidopsis Thaliana and Its Functional Implications. J.Biol.Chem. V. 286 36108 2011.
ISSN: ISSN 0021-9258
PubMed: 21865170
DOI: 10.1074/JBC.M111.275974
Page generated: Sat Aug 9 05:46:33 2025

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