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Chlorine in PDB 5bru: Catalytic Improvement of An Artificial Metalloenzyme By Computational Design

Enzymatic activity of Catalytic Improvement of An Artificial Metalloenzyme By Computational Design

All present enzymatic activity of Catalytic Improvement of An Artificial Metalloenzyme By Computational Design:
4.2.1.1;

Protein crystallography data

The structure of Catalytic Improvement of An Artificial Metalloenzyme By Computational Design, PDB code: 5bru was solved by T.Heinisch, M.Pellizzoni, M.Duerrenberger, C.E.Tinberg, V.Koehler, J.Klehr, D.Haeussinger, D.Baker, T.R.Ward, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 70.11 / 1.60
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.308, 41.689, 72.343, 90.00, 104.26, 90.00
R / Rfree (%) 13.7 / 19.4

Other elements in 5bru:

The structure of Catalytic Improvement of An Artificial Metalloenzyme By Computational Design also contains other interesting chemical elements:

Zinc (Zn) 1 atom
Iridium (Ir) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Catalytic Improvement of An Artificial Metalloenzyme By Computational Design (pdb code 5bru). 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 Catalytic Improvement of An Artificial Metalloenzyme By Computational Design, PDB code: 5bru:

Chlorine binding site 1 out of 1 in 5bru

Go back to Chlorine Binding Sites List in 5bru
Chlorine binding site 1 out of 1 in the Catalytic Improvement of An Artificial Metalloenzyme By Computational Design


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Catalytic Improvement of An Artificial Metalloenzyme By Computational Design within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl302

b:48.4
occ:1.00
 CL A:8TH302 0.0 48.4 1.0
IR A:8TH302 2.3 34.3 1.0
O3 A:8TH302 2.9 48.2 1.0
N21 A:8TH302 3.0 28.0 1.0
N3 A:8TH302 3.1 37.1 1.0
O4 A:8TH302 3.2 56.2 1.0
S2 A:8TH302 3.2 45.2 1.0
C40 A:8TH302 3.3 39.8 1.0
C24 A:8TH302 3.5 32.0 1.0
C5 A:8TH302 3.6 39.2 1.0
C6 A:8TH302 3.7 46.3 1.0
C7 A:8TH302 3.7 41.7 1.0
C22 A:8TH302 3.9 28.9 1.0
C3 A:8TH302 4.1 42.6 1.0
C21 A:8TH302 4.1 35.1 1.0
C8 A:8TH302 4.1 36.5 1.0
C9 A:8TH302 4.3 40.0 1.0
C1 A:8TH302 4.5 43.6 1.0
C41 A:8TH302 4.5 37.0 1.0
O A:HOH561 4.6 39.2 1.0
C25 A:8TH302 4.6 27.5 1.0
O A:HOH548 4.7 32.4 1.0
C4 A:8TH302 4.7 52.8 1.0
C23 A:8TH302 4.9 28.1 1.0
C13 A:8TH302 5.0 55.0 1.0

Reference:

T.Heinisch, M.Pellizzoni, M.Durrenberger, C.E.Tinberg, V.Kohler, J.Klehr, D.Haussinger, D.Baker, T.R.Ward. Improving the Catalytic Performance of An Artificial Metalloenzyme By Computational Design. J.Am.Chem.Soc. V. 137 10414 2015.
ISSN: ESSN 1520-5126
PubMed: 26226626
DOI: 10.1021/JACS.5B06622
Page generated: Sat Jul 12 00:29:25 2025

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