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Argon in PDB 6zmc: Structure of the Trna-Monooxygenase Enzyme Miae Frozen Under 2000 Bar Using the High Pressure Freezing Method

Protein crystallography data

The structure of Structure of the Trna-Monooxygenase Enzyme Miae Frozen Under 2000 Bar Using the High Pressure Freezing Method, PDB code: 6zmc was solved by P.Carpentier, M.Atta, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.52 / 2.50
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 117.388, 51.909, 78.978, 90.00, 90.36, 90.00
R / Rfree (%) 18.2 / 24.5

Other elements in 6zmc:

The structure of Structure of the Trna-Monooxygenase Enzyme Miae Frozen Under 2000 Bar Using the High Pressure Freezing Method also contains other interesting chemical elements:

Iron (Fe) 4 atoms
Calcium (Ca) 2 atoms
Chlorine (Cl) 1 atom

Argon Binding Sites:

The binding sites of Argon atom in the Structure of the Trna-Monooxygenase Enzyme Miae Frozen Under 2000 Bar Using the High Pressure Freezing Method (pdb code 6zmc). This binding sites where shown within 5.0 Angstroms radius around Argon atom.
In total only one binding site of Argon was determined in the Structure of the Trna-Monooxygenase Enzyme Miae Frozen Under 2000 Bar Using the High Pressure Freezing Method, PDB code: 6zmc:

Argon binding site 1 out of 1 in 6zmc

Go back to Argon Binding Sites List in 6zmc
Argon binding site 1 out of 1 in the Structure of the Trna-Monooxygenase Enzyme Miae Frozen Under 2000 Bar Using the High Pressure Freezing Method


Mono view


Stereo pair view

A full contact list of Argon with other atoms in the Ar binding site number 1 of Structure of the Trna-Monooxygenase Enzyme Miae Frozen Under 2000 Bar Using the High Pressure Freezing Method within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Ar304

b:89.2
occ:1.00
OH C:TYR144 3.4 69.7 1.0
CD2 C:LEU30 3.7 68.6 1.0
CD1 C:LEU140 3.7 63.1 1.0
CE2 C:TYR144 3.7 68.0 1.0
O C:GLN27 3.9 61.3 1.0
CZ C:TYR144 3.9 73.5 1.0
CB C:GLN27 4.0 59.1 1.0
CG C:GLN27 4.1 66.6 1.0
CD2 C:LEU140 4.1 76.9 1.0
CG C:LEU31 4.1 76.6 1.0
CD2 C:LEU31 4.2 83.1 1.0
CB C:LEU30 4.3 68.7 1.0
CA C:GLN27 4.3 67.7 1.0
CG C:LEU30 4.4 68.1 1.0
CG C:LEU140 4.5 67.8 1.0
C C:GLN27 4.5 60.9 1.0
N C:LEU31 4.6 61.2 1.0
OE1 C:GLN27 4.7 67.5 1.0
CD2 C:TYR144 4.8 74.8 1.0
CD2 C:LEU136 4.8 69.5 1.0
CD C:GLN27 4.8 70.3 1.0
CD1 C:LEU31 5.0 84.8 1.0
CA C:LEU31 5.0 67.1 1.0
CD1 C:LEU136 5.0 64.6 1.0
CE1 C:TYR144 5.0 77.1 1.0

Reference:

P.Carpentier, C.Lepretre, C.Basset, T.Douki, S.Torelli, V.Duarte, D.Hamdane, M.Fontecave, M.Atta. Structural, Biochemical and Functional Analyses of Trna-Monooxygenase Enzyme Miae From Pseudomonas Putida Provide Insights Into Trna/Miae Interaction. Nucleic Acids Res. V. 48 9918 2020.
ISSN: ESSN 1362-4962
PubMed: 32785618
DOI: 10.1093/NAR/GKAA667
Page generated: Sat Dec 12 01:35:50 2020

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