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Sodium in PDB 5lb9: Structure of the T175V ETR1P Mutant in the Monoclinic Form P21

Enzymatic activity of Structure of the T175V ETR1P Mutant in the Monoclinic Form P21

All present enzymatic activity of Structure of the T175V ETR1P Mutant in the Monoclinic Form P21:
1.3.1.10; 1.3.1.38;

Protein crystallography data

The structure of Structure of the T175V ETR1P Mutant in the Monoclinic Form P21, PDB code: 5lb9 was solved by T.Wagner, R.G.Rosenthal, B.Voegeli, S.Shima, T.J.Erb, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.98 / 2.10
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 67.416, 101.861, 81.593, 90.00, 101.01, 90.00
R / Rfree (%) 15.2 / 18.6

Sodium Binding Sites:

The binding sites of Sodium atom in the Structure of the T175V ETR1P Mutant in the Monoclinic Form P21 (pdb code 5lb9). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 3 binding sites of Sodium where determined in the Structure of the T175V ETR1P Mutant in the Monoclinic Form P21, PDB code: 5lb9:
Jump to Sodium binding site number: 1; 2; 3;

Sodium binding site 1 out of 3 in 5lb9

Go back to Sodium Binding Sites List in 5lb9
Sodium binding site 1 out of 3 in the Structure of the T175V ETR1P Mutant in the Monoclinic Form P21


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Structure of the T175V ETR1P Mutant in the Monoclinic Form P21 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na412

b:44.4
occ:1.00
O2 A:SO4402 2.2 61.5 0.7
O A:HOH631 2.8 36.8 1.0
N A:SER309 3.0 24.8 1.0
CB A:SER309 3.4 34.0 1.0
OG A:SER309 3.4 36.6 1.0
N A:THR308 3.4 22.7 1.0
S A:SO4402 3.6 65.2 0.7
CA A:SER309 3.8 32.3 1.0
CB A:PRO307 3.8 32.9 1.0
CB A:THR308 3.8 31.6 1.0
C A:THR308 3.9 25.1 1.0
CA A:THR308 3.9 28.2 1.0
C A:PRO307 3.9 24.4 1.0
CA A:PRO307 4.2 28.8 1.0
O3 A:SO4402 4.2 66.6 0.7
O4 A:SO4402 4.2 66.6 0.7
O1 A:SO4402 4.6 68.8 0.7
O A:PRO307 4.7 25.2 1.0
OG1 A:THR308 4.7 31.0 1.0
CG2 A:THR308 4.8 26.3 1.0

Sodium binding site 2 out of 3 in 5lb9

Go back to Sodium Binding Sites List in 5lb9
Sodium binding site 2 out of 3 in the Structure of the T175V ETR1P Mutant in the Monoclinic Form P21


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of Structure of the T175V ETR1P Mutant in the Monoclinic Form P21 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Na407

b:47.2
occ:1.00
O4 B:SO4406 2.3 72.7 1.0
N B:ALA201 3.2 29.3 1.0
O B:HOH700 3.4 28.7 1.0
S B:SO4406 3.5 60.2 1.0
CA B:SER200 3.8 25.4 1.0
CB B:SER200 3.8 26.6 1.0
O3 B:SO4406 3.8 62.1 1.0
O1 B:SO4406 3.9 66.3 1.0
CB B:ALA201 3.9 31.4 1.0
C B:SER200 4.0 24.4 1.0
CA B:ALA201 4.2 32.3 1.0
O B:HOH605 4.4 48.3 1.0
O B:HOH800 4.7 38.3 1.0
O2 B:SO4406 4.8 48.3 1.0
OG B:SER200 4.9 26.8 1.0

Sodium binding site 3 out of 3 in 5lb9

Go back to Sodium Binding Sites List in 5lb9
Sodium binding site 3 out of 3 in the Structure of the T175V ETR1P Mutant in the Monoclinic Form P21


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 3 of Structure of the T175V ETR1P Mutant in the Monoclinic Form P21 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Na408

b:50.1
occ:1.00
O2 B:SO4405 2.3 59.8 0.7
O B:HOH662 2.8 36.8 1.0
N B:SER309 3.2 26.0 1.0
N B:THR308 3.5 28.2 1.0
S B:SO4405 3.6 66.8 0.7
CB B:SER309 3.6 41.2 1.0
OG B:SER309 3.6 37.0 1.0
O B:HOH782 3.9 58.2 1.0
CB B:THR308 3.9 29.7 1.0
CB B:PRO307 3.9 32.6 1.0
CA B:SER309 4.0 29.1 1.0
O3 B:SO4405 4.0 68.7 0.7
CA B:THR308 4.0 30.2 1.0
C B:PRO307 4.1 26.8 1.0
C B:THR308 4.1 29.6 1.0
O1 B:SO4405 4.1 64.3 0.7
CA B:PRO307 4.2 30.1 1.0
O B:HOH615 4.3 55.6 1.0
O4 B:SO4405 4.7 63.0 0.7
OG1 B:THR308 4.7 32.2 1.0
O B:PRO307 4.9 30.5 1.0
CG2 B:THR308 4.9 30.0 1.0

Reference:

R.G.Rosenthal, B.Vogeli, T.Wagner, S.Shima, T.J.Erb. A Conserved Threonine Prevents Self-Intoxication of Enoyl-Thioester Reductases. Nat. Chem. Biol. V. 13 745 2017.
ISSN: ESSN 1552-4469
PubMed: 28504678
DOI: 10.1038/NCHEMBIO.2375
Page generated: Mon Oct 7 22:19:47 2024

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