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Chlorine in PDB 4x8i: De Novo Crystal Structure of the Pyrococcus Furiosus TET3 Aminopeptidase

Enzymatic activity of De Novo Crystal Structure of the Pyrococcus Furiosus TET3 Aminopeptidase

All present enzymatic activity of De Novo Crystal Structure of the Pyrococcus Furiosus TET3 Aminopeptidase:
3.4.11.15;

Protein crystallography data

The structure of De Novo Crystal Structure of the Pyrococcus Furiosus TET3 Aminopeptidase, PDB code: 4x8i was solved by M.Colombo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.06 / 2.50
Space group I 41 2 2
Cell size a, b, c (Å), α, β, γ (°) 203.908, 203.908, 112.443, 90.00, 90.00, 90.00
R / Rfree (%) 17.8 / 21.8

Other elements in 4x8i:

The structure of De Novo Crystal Structure of the Pyrococcus Furiosus TET3 Aminopeptidase also contains other interesting chemical elements:

Cobalt (Co) 3 atoms
Zinc (Zn) 3 atoms
Gadolinium (Gd) 11 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the De Novo Crystal Structure of the Pyrococcus Furiosus TET3 Aminopeptidase (pdb code 4x8i). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the De Novo Crystal Structure of the Pyrococcus Furiosus TET3 Aminopeptidase, PDB code: 4x8i:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in 4x8i

Go back to Chlorine Binding Sites List in 4x8i
Chlorine binding site 1 out of 3 in the De Novo Crystal Structure of the Pyrococcus Furiosus TET3 Aminopeptidase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of De Novo Crystal Structure of the Pyrococcus Furiosus TET3 Aminopeptidase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl403

b:57.3
occ:1.00
ZN A:ZN401 2.3 31.2 1.0
OD2 A:ASP230 2.4 51.1 1.0
O A:HOH577 2.4 41.0 1.0
OE1 A:GLU207 2.6 50.5 1.0
O A:GLY288 3.0 42.9 1.0
CG A:ASP230 3.3 47.0 1.0
CO A:CO402 3.3 28.0 1.0
CD A:GLU207 3.4 45.0 1.0
OE2 A:GLU207 3.4 46.2 1.0
OD1 A:ASP230 3.6 53.7 1.0
NE2 A:HIS63 4.1 37.0 1.0
OD1 A:ASP177 4.2 42.5 1.0
C A:GLY288 4.2 36.9 1.0
CB A:ASP230 4.4 43.0 1.0
OE1 A:GLU208 4.5 42.9 1.0
CD2 A:HIS63 4.6 38.8 1.0
OD2 A:ASP177 4.6 38.8 1.0
OE2 A:GLU208 4.6 35.9 1.0
CD A:GLU208 4.7 37.7 1.0
CA A:THR289 4.7 39.2 1.0
CG A:ASP177 4.8 38.7 1.0
CG A:GLU207 4.8 43.2 1.0
CG2 A:THR289 4.9 34.0 1.0
N A:THR289 4.9 36.2 1.0
CE1 A:HIS63 5.0 37.4 1.0

Chlorine binding site 2 out of 3 in 4x8i

Go back to Chlorine Binding Sites List in 4x8i
Chlorine binding site 2 out of 3 in the De Novo Crystal Structure of the Pyrococcus Furiosus TET3 Aminopeptidase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of De Novo Crystal Structure of the Pyrococcus Furiosus TET3 Aminopeptidase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl403

b:44.8
occ:1.00
OD2 B:ASP230 2.3 52.6 1.0
ZN B:ZN401 2.4 42.8 1.0
OE2 B:GLU207 2.7 49.2 1.0
O B:HOH558 2.9 46.7 1.0
O B:GLY288 2.9 46.0 1.0
CG B:ASP230 3.3 48.4 1.0
OE1 B:GLU207 3.3 46.5 1.0
O B:HOH555 3.3 55.1 1.0
CD B:GLU207 3.4 45.2 1.0
OD1 B:ASP230 3.7 45.7 1.0
CO B:CO402 3.7 35.4 1.0
NE2 B:HIS63 4.1 39.7 1.0
C B:GLY288 4.1 41.7 1.0
CB B:ASP230 4.4 48.3 1.0
OD1 B:ASP177 4.4 44.4 1.0
OD2 B:ASP177 4.7 43.8 1.0
OE2 B:GLU208 4.7 37.8 1.0
CD2 B:HIS63 4.7 39.6 1.0
CA B:THR289 4.7 40.8 1.0
CG2 B:THR289 4.8 37.8 1.0
CG B:GLU207 4.8 40.5 1.0
N B:THR289 4.9 41.5 1.0
CG B:ASP177 4.9 42.5 1.0

Chlorine binding site 3 out of 3 in 4x8i

Go back to Chlorine Binding Sites List in 4x8i
Chlorine binding site 3 out of 3 in the De Novo Crystal Structure of the Pyrococcus Furiosus TET3 Aminopeptidase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of De Novo Crystal Structure of the Pyrococcus Furiosus TET3 Aminopeptidase within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl403

b:49.3
occ:1.00
ZN C:ZN401 2.4 40.7 1.0
OD2 C:ASP230 2.5 62.8 1.0
OE1 C:GLU207 2.6 53.9 1.0
O C:GLY288 2.8 47.6 1.0
O C:HOH554 3.0 67.5 1.0
O C:HOH556 3.2 68.8 1.0
CG C:ASP230 3.3 56.9 1.0
CO C:CO402 3.5 33.2 1.0
CD C:GLU207 3.5 49.9 1.0
OE2 C:GLU207 3.5 50.3 1.0
OD1 C:ASP230 3.6 57.4 1.0
C C:GLY288 4.0 42.2 1.0
NE2 C:HIS63 4.2 37.0 1.0
OD1 C:ASP177 4.4 41.4 1.0
OE2 C:GLU208 4.4 44.3 1.0
CB C:ASP230 4.4 52.3 1.0
OD2 C:ASP177 4.6 46.3 1.0
CA C:THR289 4.7 40.2 1.0
N C:THR289 4.8 40.2 1.0
CD2 C:HIS63 4.8 37.3 1.0
CG2 C:THR289 4.8 31.8 1.0
CD C:GLU208 4.9 41.9 1.0
OE1 C:GLU208 4.9 44.0 1.0
CG C:ASP177 4.9 41.2 1.0
CG C:GLU207 4.9 46.6 1.0

Reference:

M.Colombo, E.Girard, B.Franzetti. Tuned By Metals: the Tet Peptidase Activity Is Controlled By 3 Metal Binding Sites. Sci Rep V. 6 20876 2016.
ISSN: ESSN 2045-2322
PubMed: 26853450
DOI: 10.1038/SREP20876
Page generated: Fri Jul 26 03:17:21 2024

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