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Chlorine in PDB 6g58: Structure of the Alanine Racemase From Staphylococcus Aureus in Complex with A Pyridoxal 5' Phosphate-Derivative

Enzymatic activity of Structure of the Alanine Racemase From Staphylococcus Aureus in Complex with A Pyridoxal 5' Phosphate-Derivative

All present enzymatic activity of Structure of the Alanine Racemase From Staphylococcus Aureus in Complex with A Pyridoxal 5' Phosphate-Derivative:
5.1.1.1;

Protein crystallography data

The structure of Structure of the Alanine Racemase From Staphylococcus Aureus in Complex with A Pyridoxal 5' Phosphate-Derivative, PDB code: 6g58 was solved by A.Hoegl, S.A.Sieber, S.Schneider, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.40 / 1.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 85.543, 106.767, 130.835, 90.00, 90.00, 90.00
R / Rfree (%) 15.1 / 17

Other elements in 6g58:

The structure of Structure of the Alanine Racemase From Staphylococcus Aureus in Complex with A Pyridoxal 5' Phosphate-Derivative also contains other interesting chemical elements:

Sodium (Na) 6 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structure of the Alanine Racemase From Staphylococcus Aureus in Complex with A Pyridoxal 5' Phosphate-Derivative (pdb code 6g58). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Structure of the Alanine Racemase From Staphylococcus Aureus in Complex with A Pyridoxal 5' Phosphate-Derivative, PDB code: 6g58:

Chlorine binding site 1 out of 1 in 6g58

Go back to Chlorine Binding Sites List in 6g58
Chlorine binding site 1 out of 1 in the Structure of the Alanine Racemase From Staphylococcus Aureus in Complex with A Pyridoxal 5' Phosphate-Derivative


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of the Alanine Racemase From Staphylococcus Aureus in Complex with A Pyridoxal 5' Phosphate-Derivative within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl405

b:39.5
occ:1.00
 NH2 B:ARG138 3.1 41.4 1.0
NE B:ARG138 3.1 34.7 1.0
O B:HOH635 3.2 25.4 1.0
CE B:LYS131 3.2 35.5 1.0
NZ B:LYS131 3.3 39.2 1.0
O B:HOH505 3.3 30.8 1.0
CG B:MET136 3.4 35.8 1.0
CZ B:ARG138 3.6 38.3 1.0
CB B:MET136 3.8 31.4 1.0
CB B:ARG138 4.0 31.3 1.0
CB B:HIS168 4.1 21.7 1.0
C7 B:EOW401 4.3 44.8 1.0
O B:LEU139 4.3 45.4 1.0
CD B:ARG138 4.3 36.0 1.0
C1 B:EOW401 4.4 32.6 1.0
CG B:ARG138 4.4 34.3 1.0
CD2 B:HIS168 4.5 28.4 1.0
C8 B:EOW401 4.5 33.6 1.0
CG B:HIS168 4.6 24.2 1.0
CD B:LYS131 4.7 28.2 1.0
O B:HOH573 4.8 35.5 1.0
CE B:MET136 4.8 40.2 1.0
O B:HOH661 4.8 22.3 1.0
N B:ARG138 4.9 31.3 1.0
SD B:MET136 4.9 34.7 1.0
NH1 B:ARG138 4.9 37.6 1.0
CA B:ARG138 4.9 34.6 1.0

Reference:

A.Hoegl, M.B.Nodwell, V.C.Kirsch, N.C.Bach, M.Pfanzelt, M.Stahl, S.Schneider, S.A.Sieber. Mining the Cellular Inventory of Pyridoxal Phosphate-Dependent Enzymes with Functionalized Cofactor Mimics. Nat Chem V. 10 1234 2018.
ISSN: ESSN 1755-4349
PubMed: 30297752
DOI: 10.1038/S41557-018-0144-2
Page generated: Sat Jul 27 23:42:51 2024

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