Sodium in PDB 4wxg: Crystal Structure of L-Serine Hydroxymethyltransferase in Complex with A Mixture of L-Allo-Threonine and Glycine

Enzymatic activity of Crystal Structure of L-Serine Hydroxymethyltransferase in Complex with A Mixture of L-Allo-Threonine and Glycine

All present enzymatic activity of Crystal Structure of L-Serine Hydroxymethyltransferase in Complex with A Mixture of L-Allo-Threonine and Glycine:
2.1.2.1;

Protein crystallography data

The structure of Crystal Structure of L-Serine Hydroxymethyltransferase in Complex with A Mixture of L-Allo-Threonine and Glycine, PDB code: 4wxg was solved by K.Hernandez, I.Zelen, G.Petrillo, I.Uson, C.Wandtke, J.Bujons, J.Joglar, T.Parella, P.Clapes, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.43 / 2.00
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 115.430, 115.430, 191.480, 90.00, 90.00, 90.00
R / Rfree (%) 17.1 / 20.3

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of L-Serine Hydroxymethyltransferase in Complex with A Mixture of L-Allo-Threonine and Glycine (pdb code 4wxg). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Crystal Structure of L-Serine Hydroxymethyltransferase in Complex with A Mixture of L-Allo-Threonine and Glycine, PDB code: 4wxg:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in 4wxg

Go back to Sodium Binding Sites List in 4wxg
Sodium binding site 1 out of 2 in the Crystal Structure of L-Serine Hydroxymethyltransferase in Complex with A Mixture of L-Allo-Threonine and Glycine


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 L-Serine Hydroxymethyltransferase in Complex with A Mixture of L-Allo-Threonine and Glycine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na502

b:40.2
occ:1.00
O A:PHE301 2.1 34.5 1.0
O A:HIS298 2.2 48.0 1.0
O A:PHE295 2.4 36.4 1.0
O A:ASN296 2.4 35.8 1.0
C A:ASN296 3.2 34.5 1.0
C A:PHE301 3.3 34.3 1.0
C A:HIS298 3.4 42.1 1.0
C A:PHE295 3.6 33.8 1.0
CA A:ASN296 3.6 36.1 1.0
N A:HIS298 3.9 40.3 1.0
N A:ASN296 4.1 33.6 1.0
N A:PHE301 4.1 36.3 1.0
CA A:PHE301 4.1 32.4 1.0
O A:HOH708 4.2 36.1 1.0
CA A:HIS298 4.2 41.5 1.0
N A:GLN297 4.2 34.3 1.0
N A:ARG302 4.2 33.9 1.0
CA A:ARG302 4.3 34.6 1.0
C A:GLN297 4.3 45.6 1.0
N A:PRO299 4.3 43.4 1.0
CA A:PRO299 4.5 38.5 1.0
CB A:PHE301 4.5 30.3 1.0
C A:PRO299 4.6 39.1 1.0
CA A:GLN297 4.7 45.8 1.0
CB A:HIS298 4.7 40.6 1.0
CA A:PHE295 4.8 31.6 1.0
O A:GLN297 4.9 44.9 1.0
O A:PRO299 5.0 37.5 1.0
CB A:ASN296 5.0 34.9 1.0

Sodium binding site 2 out of 2 in 4wxg

Go back to Sodium Binding Sites List in 4wxg
Sodium binding site 2 out of 2 in the Crystal Structure of L-Serine Hydroxymethyltransferase in Complex with A Mixture of L-Allo-Threonine and Glycine


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of Crystal Structure of L-Serine Hydroxymethyltransferase in Complex with A Mixture of L-Allo-Threonine and Glycine within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Na502

b:60.1
occ:1.00
O C:PHE301 2.0 58.0 1.0
O C:HIS298 2.3 72.6 1.0
O C:ASN296 2.4 61.4 1.0
O C:PHE295 2.6 54.1 1.0
C C:ASN296 3.1 65.3 1.0
C C:PHE301 3.3 56.0 1.0
C C:HIS298 3.5 67.0 1.0
CA C:ASN296 3.5 54.6 1.0
C C:PHE295 3.7 54.1 1.0
N C:ASN296 4.0 50.6 1.0
N C:GLN297 4.1 65.0 1.0
N C:ARG302 4.2 58.2 1.0
CA C:ARG302 4.2 53.6 1.0
N C:HIS298 4.2 65.3 1.0
CA C:PHE301 4.2 60.1 1.0
N C:PHE301 4.2 59.9 1.0
C C:GLN297 4.3 62.2 1.0
CA C:HIS298 4.4 62.7 1.0
N C:PRO299 4.4 68.1 1.0
CB C:PHE301 4.4 56.0 1.0
CA C:PRO299 4.4 62.7 1.0
CA C:GLN297 4.6 61.9 1.0
C C:PRO299 4.7 56.8 1.0
O C:GLN297 4.7 68.2 1.0
O C:PRO299 4.8 64.0 1.0
CB C:ASN296 4.9 55.5 1.0
OD1 C:ASN296 4.9 59.9 1.0
CB C:HIS298 5.0 59.4 1.0

Reference:

K.Hernandez, I.Zelen, G.Petrillo, I.Uson, C.M.Wandtke, J.Bujons, J.Joglar, T.Parella, P.Clapes. Engineered L-Serine Hydroxymethyltransferase From Streptococcus Thermophilus For the Synthesis of Alpha , Alpha-Dialkyl-Alpha-Amino Acids. Angew.Chem.Int.Ed.Engl. 2015.
ISSN: ESSN 1521-3773
PubMed: 25611820
DOI: 10.1002/ANIE.201411484
Page generated: Tue Dec 15 09:43:17 2020

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