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Chlorine in PDB 6ggl: Crystal Structure of COTB2 Variant F107A

Enzymatic activity of Crystal Structure of COTB2 Variant F107A

All present enzymatic activity of Crystal Structure of COTB2 Variant F107A:
4.2.3.146;

Protein crystallography data

The structure of Crystal Structure of COTB2 Variant F107A, PDB code: 6ggl was solved by R.Driller, S.Janke, M.Fuchs, E.Warner, A.R.Mhashal, D.T.Major, M.Christmann, T.Brueck, B.Loll, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.50 / 1.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 61.410, 100.080, 107.940, 90.00, 90.00, 90.00
R / Rfree (%) 17.5 / 20.6

Other elements in 6ggl:

The structure of Crystal Structure of COTB2 Variant F107A also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of COTB2 Variant F107A (pdb code 6ggl). 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 Crystal Structure of COTB2 Variant F107A, PDB code: 6ggl:

Chlorine binding site 1 out of 1 in 6ggl

Go back to Chlorine Binding Sites List in 6ggl
Chlorine binding site 1 out of 1 in the Crystal Structure of COTB2 Variant F107A


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of COTB2 Variant F107A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl402

b:73.8
occ:1.00
O B:HOH622 3.4 37.9 1.0
O A:HOH624 3.9 39.0 1.0
CB A:GLU144 4.6 24.2 1.0
CG A:GLU144 4.7 24.4 1.0
CG2 B:VAL141 4.7 33.2 1.0
O A:HOH557 4.7 28.7 1.0
O A:GLU140 4.8 23.2 1.0

Reference:

R.Driller, S.Janke, M.Fuchs, E.Warner, A.R.Mhashal, D.T.Major, M.Christmann, T.Bruck, B.Loll. Towards A Comprehensive Understanding of the Structural Dynamics of A Bacterial Diterpene Synthase During Catalysis. Nat Commun V. 9 3971 2018.
ISSN: ESSN 2041-1723
PubMed: 30266969
DOI: 10.1038/S41467-018-06325-8
Page generated: Sat Jul 27 23:56:57 2024

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