Atomistry » Zinc » PDB 5bqm-5c2e » 5bru
Atomistry »
  Zinc »
    PDB 5bqm-5c2e »
      5bru »

Zinc 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:

Chlorine (Cl) 1 atom
Iridium (Ir) 1 atom

Zinc Binding Sites:

The binding sites of Zinc 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 Zinc atom.
In total only one binding site of Zinc was determined in the Catalytic Improvement of An Artificial Metalloenzyme By Computational Design, PDB code: 5bru:

Zinc binding site 1 out of 1 in 5bru

Go back to Zinc Binding Sites List in 5bru
Zinc 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 Zinc with other atoms in the Zn 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:Zn301

b:8.4
occ:1.00
N2 A:8TH302 2.0 7.0 1.0
NE2 A:HIS94 2.0 7.4 1.0
ND1 A:HIS119 2.0 8.3 1.0
NE2 A:HIS96 2.1 8.9 1.0
CD2 A:HIS94 2.9 7.8 1.0
CE1 A:HIS119 2.9 7.7 1.0
CD2 A:HIS96 3.0 8.2 1.0
O2 A:8TH302 3.1 9.0 1.0
S1 A:8TH302 3.1 10.1 1.0
CE1 A:HIS96 3.1 9.0 1.0
CE1 A:HIS94 3.1 7.0 1.0
CG A:HIS119 3.1 7.3 1.0
CB A:HIS119 3.6 8.0 1.0
O A:HOH546 3.8 19.0 1.0
OG1 A:THR198 3.9 9.3 1.0
O1 A:8TH302 4.0 9.6 1.0
OE1 A:GLU106 4.0 13.1 1.0
NE2 A:HIS119 4.1 8.0 1.0
CG A:HIS94 4.1 8.0 1.0
ND1 A:HIS94 4.1 8.1 1.0
ND1 A:HIS96 4.2 10.0 1.0
CG A:HIS96 4.2 8.5 1.0
CD2 A:HIS119 4.2 8.4 1.0
C32 A:8TH302 4.2 11.3 1.0
C29 A:8TH302 4.9 15.1 1.0
C31 A:8TH302 4.9 14.5 1.0
CD A:GLU106 5.0 11.5 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: Wed Dec 16 06:05:02 2020

Last articles

Zn in 7VD8
Zn in 7V1R
Zn in 7V1Q
Zn in 7VPF
Zn in 7T85
Zn in 7T5F
Zn in 7NF9
Zn in 7M4M
Zn in 7M4O
Zn in 7M4N
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy