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Chlorine in PDB 6zmb: Structure of the Native Trna-Monooxygenase Enzyme Miae

Protein crystallography data

The structure of Structure of the Native Trna-Monooxygenase Enzyme Miae, PDB code: 6zmb 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) 46.75 / 1.70
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 116.797, 50.929, 76.258, 90.00, 91.00, 90.00
R / Rfree (%) 18.8 / 21.7

Other elements in 6zmb:

The structure of Structure of the Native Trna-Monooxygenase Enzyme Miae also contains other interesting chemical elements:

Iron (Fe) 4 atoms
Calcium (Ca) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structure of the Native Trna-Monooxygenase Enzyme Miae (pdb code 6zmb). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Structure of the Native Trna-Monooxygenase Enzyme Miae, PDB code: 6zmb:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 6zmb

Go back to Chlorine Binding Sites List in 6zmb
Chlorine binding site 1 out of 2 in the Structure of the Native Trna-Monooxygenase Enzyme Miae


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 Native Trna-Monooxygenase Enzyme Miae within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl303

b:72.2
occ:1.00
O B:GLU21 3.2 30.9 1.0
N B:ALA25 4.0 27.2 1.0
C B:GLU21 4.0 30.3 1.0
CB B:ALA25 4.0 32.2 1.0
CB B:LEU24 4.0 30.2 1.0
CA B:GLU21 4.1 32.7 1.0
CA B:ALA25 4.4 34.3 1.0
C B:LEU24 4.4 32.8 1.0
CB B:GLU21 4.5 35.3 1.0
CG B:GLU21 4.6 54.1 1.0
CA B:LEU24 4.8 29.7 1.0

Chlorine binding site 2 out of 2 in 6zmb

Go back to Chlorine Binding Sites List in 6zmb
Chlorine binding site 2 out of 2 in the Structure of the Native Trna-Monooxygenase Enzyme Miae


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Structure of the Native Trna-Monooxygenase Enzyme Miae within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl304

b:38.3
occ:1.00
NH2 C:ARG67 3.1 32.3 1.0
NH1 B:ARG67 3.1 31.4 1.0
CD C:ARG67 3.8 24.9 1.0
O B:HOH488 3.8 46.0 1.0
CD B:ARG67 3.9 21.2 1.0
CB B:ARG67 3.9 23.5 1.0
CB C:ARG67 4.0 25.6 1.0
O2 C:PGE305 4.1 47.6 1.0
CZ C:ARG67 4.2 29.7 1.0
CZ B:ARG67 4.3 27.2 1.0
CG C:ARG67 4.3 25.4 1.0
CG B:ARG67 4.3 20.7 1.0
NE C:ARG67 4.5 25.8 1.0
CG2 B:VAL71 4.5 23.9 1.0
NE B:ARG67 4.5 23.9 1.0
CG2 C:VAL71 4.6 27.4 1.0
C2 C:PGE305 4.6 55.7 1.0
O B:ARG67 4.7 24.9 1.0
O C:ARG67 4.9 23.7 1.0
CA B:ARG67 4.9 21.7 1.0
CA C:ARG67 4.9 18.9 1.0
C B:ARG67 5.0 23.3 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: Mon Jul 29 18:06:44 2024

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