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Potassium in PDB 3s29: 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: 3s29 was solved by Y.I.Zheng, R.M.Garavito, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.96 / 2.85
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 277.160, 261.500, 161.100, 90.00, 109.27, 90.00
R / Rfree (%) 18.5 / 23.4

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 3s29). 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: 3s29:
Jump to Potassium binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Potassium binding site 1 out of 8 in 3s29

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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:72.1
occ:1.00
 O A:LEU194 2.4 48.1 1.0
O A:HIS187 2.5 49.8 1.0
O A:LEU184 2.6 48.0 1.0
O A:ARG185 2.6 63.3 1.0
O A:LEU196 2.7 62.6 1.0
C A:ARG185 3.1 61.0 1.0
C A:HIS187 3.5 52.4 1.0
C A:LEU194 3.5 46.9 1.0
N A:HIS187 3.5 54.8 1.0
OD1 A:ASN193 3.6 66.5 1.0
CA A:ARG185 3.6 57.5 1.0
C A:LEU184 3.6 49.9 1.0
N A:LEU194 3.8 52.3 1.0
C A:LEU196 3.9 57.3 1.0
CA A:HIS187 3.9 53.6 1.0
CG A:ASN193 4.0 65.9 1.0
C A:LEU186 4.0 58.5 1.0
N A:LEU186 4.0 57.3 1.0
ND2 A:ASN193 4.0 64.2 1.0
N A:LEU196 4.1 47.4 1.0
N A:ARG185 4.1 54.3 1.0
CA A:LEU194 4.1 50.9 1.0
CB A:HIS187 4.2 51.0 1.0
CA A:LEU186 4.4 57.9 1.0
CA A:LEU196 4.5 50.6 1.0
O A:LEU186 4.5 58.2 1.0
N A:MET195 4.6 46.4 1.0
C A:MET195 4.6 49.5 1.0
N A:SER188 4.7 57.3 1.0
C A:ASN193 4.8 54.3 1.0
CB A:MET195 4.8 47.5 1.0
CB A:LEU194 4.8 49.3 1.0
CA A:MET195 4.9 49.7 1.0
CA A:LEU184 4.9 48.4 1.0
N A:SER197 4.9 59.7 1.0

Potassium binding site 2 out of 8 in 3s29

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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:99.3
occ:1.00
 O B:HIS187 1.9 84.8 1.0
O B:LEU194 2.6 67.7 1.0
C B:HIS187 3.1 80.0 1.0
O B:LEU196 3.4 72.3 1.0
N B:LEU194 3.4 68.5 1.0
O B:ARG185 3.4 77.0 1.0
O B:LEU184 3.6 69.1 1.0
C B:LEU194 3.7 67.8 1.0
CG B:ASN193 3.7 83.1 1.0
OD1 B:ASN193 3.8 86.4 1.0
O B:LEU186 3.8 78.8 1.0
ND2 B:ASN193 3.8 77.5 1.0
N B:HIS187 3.9 81.0 1.0
C B:LEU186 3.9 83.0 1.0
CA B:HIS187 4.0 75.3 1.0
C B:ARG185 4.1 78.3 1.0
CA B:LEU194 4.1 65.0 1.0
N B:SER188 4.1 85.7 1.0
CA B:ASN193 4.2 75.0 1.0
CB B:SER188 4.2 85.6 1.0
C B:ASN193 4.2 72.2 1.0
CB B:ASN193 4.3 80.5 1.0
CA B:SER188 4.3 79.7 1.0
C B:LEU196 4.5 69.8 1.0
CB B:HIS187 4.5 72.3 1.0
C B:LEU184 4.6 70.4 1.0
N B:LEU186 4.7 76.2 1.0
N B:LEU196 4.7 58.4 1.0
CB B:LEU194 4.7 59.5 1.0
CA B:LEU186 4.8 81.0 1.0
CA B:ARG185 4.8 78.3 1.0
N B:MET195 4.9 62.1 1.0

Potassium binding site 3 out of 8 in 3s29

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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:75.6
occ:1.00
 O C:LEU196 2.2 56.6 1.0
O C:ARG185 2.3 63.5 1.0
O C:LEU184 2.7 52.5 1.0
C C:ARG185 2.7 56.6 1.0
O C:LEU194 2.8 46.1 1.0
CA C:ARG185 3.1 52.2 1.0
O C:HIS187 3.3 56.8 1.0
C C:LEU196 3.4 53.6 1.0
OD1 C:ASN193 3.5 64.3 1.0
C C:LEU184 3.6 52.5 1.0
N C:LEU186 3.7 55.6 1.0
N C:HIS187 3.8 50.8 1.0
N C:ARG185 3.8 51.9 1.0
N C:LEU196 3.8 48.0 1.0
C C:LEU194 4.0 48.2 1.0
CG C:ASN193 4.0 62.2 1.0
CA C:LEU196 4.1 51.3 1.0
C C:LEU186 4.1 52.3 1.0
ND2 C:ASN193 4.1 62.3 1.0
C C:HIS187 4.2 57.2 1.0
CA C:LEU186 4.3 54.5 1.0
N C:LEU194 4.4 59.5 1.0
CA C:HIS187 4.4 52.4 1.0
N C:SER197 4.4 56.5 1.0
CB C:ARG185 4.5 57.7 1.0
CB C:LEU196 4.5 51.6 1.0
CB C:HIS187 4.6 52.1 1.0
CA C:SER197 4.6 58.1 1.0
C C:MET195 4.6 46.1 1.0
CB C:MET195 4.7 43.2 1.0
CG C:ARG185 4.7 64.8 1.0
CA C:LEU194 4.8 53.1 1.0
O C:LEU186 4.8 54.4 1.0
N C:MET195 4.9 47.2 1.0
CA C:MET195 5.0 44.9 1.0
CA C:LEU184 5.0 46.5 1.0

Potassium binding site 4 out of 8 in 3s29

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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:81.1
occ:1.00
 O D:ARG185 2.5 65.0 1.0
O D:LEU196 2.5 57.6 1.0
O D:HIS187 2.7 59.8 1.0
O D:LEU194 2.8 53.7 1.0
OD1 D:ASN193 2.8 70.3 1.0
O D:LEU184 2.8 56.9 1.0
C D:ARG185 3.1 60.2 1.0
CG D:ASN193 3.6 67.0 1.0
CA D:ARG185 3.6 53.6 1.0
N D:HIS187 3.7 55.7 1.0
C D:LEU196 3.7 55.9 1.0
C D:HIS187 3.7 59.5 1.0
ND2 D:ASN193 3.8 63.9 1.0
C D:LEU186 3.8 54.4 1.0
C D:LEU184 3.9 56.0 1.0
C D:LEU194 3.9 55.8 1.0
N D:LEU186 3.9 58.3 1.0
N D:LEU194 4.0 55.4 1.0
CA D:HIS187 4.2 57.8 1.0
N D:ARG185 4.2 56.4 1.0
O D:LEU186 4.2 56.8 1.0
N D:LEU196 4.2 51.1 1.0
CA D:LEU186 4.3 57.2 1.0
CA D:LEU196 4.5 55.4 1.0
CA D:LEU194 4.5 57.0 1.0
CB D:HIS187 4.6 54.1 1.0
N D:SER197 4.7 59.0 1.0
CB D:ASN193 4.8 63.3 1.0
CA D:SER197 4.8 62.3 1.0
C D:ASN193 4.9 56.8 1.0
N D:SER188 4.9 55.9 1.0
C D:MET195 4.9 51.3 1.0
CB D:ARG185 5.0 55.4 1.0

Potassium binding site 5 out of 8 in 3s29

Go back to Potassium Binding Sites List in 3s29
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:79.1
occ:1.00
 O E:LEU196 2.3 57.1 1.0
O E:LEU184 2.4 53.8 1.0
O E:LEU194 2.4 53.3 1.0
O E:ARG185 2.6 62.8 1.0
C E:ARG185 3.0 55.1 1.0
CA E:ARG185 3.2 50.2 1.0
O E:HIS187 3.2 59.4 1.0
C E:LEU184 3.4 53.5 1.0
C E:LEU196 3.4 53.9 1.0
OD1 E:ASN193 3.5 65.5 1.0
C E:LEU194 3.6 52.5 1.0
N E:LEU196 3.7 50.5 1.0
N E:ARG185 3.7 48.7 1.0
N E:HIS187 3.9 53.4 1.0
N E:LEU186 3.9 51.1 1.0
CG E:ASN193 4.0 66.8 1.0
CA E:LEU196 4.0 49.5 1.0
N E:LEU194 4.0 56.4 1.0
ND2 E:ASN193 4.1 67.6 1.0
C E:HIS187 4.2 56.7 1.0
C E:LEU186 4.2 53.7 1.0
CA E:HIS187 4.4 53.7 1.0
C E:MET195 4.4 49.0 1.0
CA E:LEU194 4.4 51.4 1.0
CB E:LEU196 4.4 54.6 1.0
CB E:MET195 4.4 49.7 1.0
CA E:LEU186 4.5 50.9 1.0
N E:SER197 4.5 63.0 1.0
CB E:HIS187 4.6 50.1 1.0
CB E:ARG185 4.6 59.5 1.0
N E:MET195 4.6 48.8 1.0
CA E:MET195 4.7 48.9 1.0
CA E:LEU184 4.7 49.0 1.0
O E:LEU186 4.9 60.1 1.0
CA E:SER197 4.9 64.0 1.0
O E:SER197 4.9 65.2 1.0
CG E:ARG185 4.9 64.9 1.0

Potassium binding site 6 out of 8 in 3s29

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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:89.5
occ:1.00
 O F:LEU196 2.5 65.9 1.0
O F:ARG185 2.6 73.6 1.0
O F:LEU194 2.6 56.8 1.0
O F:LEU184 2.7 59.1 1.0
O F:HIS187 2.8 69.2 1.0
OD1 F:ASN193 2.8 78.0 1.0
C F:ARG185 3.1 65.0 1.0
CA F:ARG185 3.5 58.9 1.0
C F:LEU184 3.7 61.4 1.0
C F:LEU196 3.7 63.9 1.0
CG F:ASN193 3.7 76.7 1.0
C F:LEU194 3.7 58.3 1.0
N F:HIS187 3.8 72.5 1.0
C F:HIS187 3.8 68.8 1.0
N F:LEU194 3.9 64.0 1.0
N F:ARG185 4.0 59.8 1.0
N F:LEU196 4.1 52.8 1.0
N F:LEU186 4.1 63.9 1.0
CA F:HIS187 4.1 67.3 1.0
ND2 F:ASN193 4.2 73.2 1.0
C F:LEU186 4.2 70.2 1.0
CB F:HIS187 4.3 64.1 1.0
CA F:LEU194 4.4 60.3 1.0
CA F:LEU196 4.4 54.2 1.0
CA F:LEU186 4.6 65.2 1.0
CB F:MET195 4.7 52.1 1.0
N F:SER197 4.7 65.7 1.0
C F:MET195 4.7 54.7 1.0
O F:LEU186 4.8 68.4 1.0
N F:MET195 4.8 55.2 1.0
C F:ASN193 4.9 68.2 1.0
CB F:ASN193 4.9 73.8 1.0
CB F:ARG185 4.9 65.3 1.0
CA F:SER197 4.9 66.9 1.0
CB F:LEU196 4.9 55.6 1.0
CA F:MET195 5.0 52.2 1.0
N F:SER188 5.0 72.6 1.0

Potassium binding site 7 out of 8 in 3s29

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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:76.4
occ:1.00
 O G:LEU196 2.2 59.0 1.0
O G:LEU184 2.4 56.8 1.0
O G:ARG185 2.4 58.7 1.0
O G:LEU194 2.7 52.6 1.0
C G:ARG185 2.7 54.2 1.0
CA G:ARG185 3.0 51.1 1.0
C G:LEU184 3.3 53.0 1.0
C G:LEU196 3.3 55.5 1.0
OD1 G:ASN193 3.4 57.2 1.0
O G:HIS187 3.4 47.6 1.0
N G:ARG185 3.6 50.4 1.0
N G:LEU196 3.6 50.1 1.0
N G:LEU186 3.7 52.5 1.0
N G:HIS187 3.7 52.1 1.0
C G:LEU194 3.9 49.9 1.0
CA G:LEU196 3.9 52.6 1.0
C G:LEU186 4.0 57.4 1.0
C G:HIS187 4.2 55.3 1.0
CG G:ASN193 4.2 64.7 1.0
CA G:HIS187 4.3 54.8 1.0
CB G:ARG185 4.3 56.5 1.0
CA G:LEU186 4.3 55.4 1.0
CB G:LEU196 4.3 47.3 1.0
C G:MET195 4.4 47.1 1.0
N G:SER197 4.5 60.7 1.0
N G:LEU194 4.5 55.6 1.0
CB G:MET195 4.5 48.0 1.0
ND2 G:ASN193 4.5 65.7 1.0
CB G:HIS187 4.6 55.1 1.0
O G:LEU186 4.6 63.8 1.0
CG G:ARG185 4.7 58.4 1.0
CA G:LEU184 4.7 47.6 1.0
CA G:SER197 4.7 64.3 1.0
CA G:MET195 4.8 44.4 1.0
CA G:LEU194 4.8 50.8 1.0
N G:MET195 4.8 50.0 1.0

Potassium binding site 8 out of 8 in 3s29

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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:74.5
occ:1.00
 O H:HIS187 2.6 55.6 1.0
O H:LEU194 2.6 45.7 1.0
O H:LEU196 2.7 58.5 1.0
O H:ARG185 2.7 62.2 1.0
OD1 H:ASN193 2.8 68.8 1.0
CG H:ASN193 3.2 64.7 1.0
ND2 H:ASN193 3.3 63.9 1.0
C H:ARG185 3.5 59.6 1.0
O H:LEU184 3.5 54.1 1.0
N H:LEU194 3.6 52.7 1.0
C H:HIS187 3.6 57.8 1.0
C H:LEU194 3.7 47.7 1.0
N H:HIS187 3.8 52.1 1.0
C H:LEU196 3.8 55.4 1.0
C H:LEU186 3.9 58.3 1.0
CA H:HIS187 4.1 53.7 1.0
O H:LEU186 4.2 67.8 1.0
CA H:ARG185 4.2 61.6 1.0
CA H:LEU194 4.2 48.3 1.0
CB H:ASN193 4.2 58.6 1.0
N H:LEU186 4.3 60.7 1.0
N H:LEU196 4.4 51.6 1.0
C H:ASN193 4.4 55.2 1.0
CA H:ASN193 4.4 51.6 1.0
CA H:LEU186 4.5 58.7 1.0
C H:LEU184 4.5 56.7 1.0
CB H:HIS187 4.6 50.0 1.0
N H:SER188 4.7 59.5 1.0
N H:SER197 4.7 61.4 1.0
CA H:LEU196 4.7 51.8 1.0
CA H:SER197 4.7 58.9 1.0
N H:ARG185 4.8 56.7 1.0
N H:MET195 4.9 47.7 1.0
C H:MET195 4.9 49.0 1.0
CG H:GLU239 5.0 54.8 1.0
CB H:LEU194 5.0 47.1 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: Mon Aug 12 09:25:05 2024

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