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Arsenic in PDB 1wy2: Crystal Structure of the Prolidase From Pyrococcus Horikoshii OT3

Enzymatic activity of Crystal Structure of the Prolidase From Pyrococcus Horikoshii OT3

All present enzymatic activity of Crystal Structure of the Prolidase From Pyrococcus Horikoshii OT3:
3.4.13.9;

Protein crystallography data

The structure of Crystal Structure of the Prolidase From Pyrococcus Horikoshii OT3, PDB code: 1wy2 was solved by H.Mizutani, N.Kunishima, Riken Structural Genomics/Proteomicsinitiative (Rsgi), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.70
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 66.697, 105.876, 106.291, 90.00, 90.00, 90.00
R / Rfree (%) 18.7 / 21

Other elements in 1wy2:

The structure of Crystal Structure of the Prolidase From Pyrococcus Horikoshii OT3 also contains other interesting chemical elements:

Magnesium (Mg) 1 atom
Zinc (Zn) 4 atoms

Arsenic Binding Sites:

The binding sites of Arsenic atom in the Crystal Structure of the Prolidase From Pyrococcus Horikoshii OT3 (pdb code 1wy2). This binding sites where shown within 5.0 Angstroms radius around Arsenic atom.
In total 2 binding sites of Arsenic where determined in the Crystal Structure of the Prolidase From Pyrococcus Horikoshii OT3, PDB code: 1wy2:
Jump to Arsenic binding site number: 1; 2;

Arsenic binding site 1 out of 2 in 1wy2

Go back to Arsenic Binding Sites List in 1wy2
Arsenic binding site 1 out of 2 in the Crystal Structure of the Prolidase From Pyrococcus Horikoshii OT3


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 1 of Crystal Structure of the Prolidase From Pyrococcus Horikoshii OT3 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:As403

b:30.5
occ:1.00
AS A:CAC403 0.0 30.5 1.0
O2 A:CAC403 1.6 28.3 1.0
O1 A:CAC403 1.7 23.3 1.0
C1 A:CAC403 1.9 29.4 1.0
C2 A:CAC403 1.9 27.1 1.0
ZN A:ZN406 3.2 18.1 1.0
ZN A:ZN405 3.3 17.2 1.0
O A:HOH1512 3.7 33.3 1.0
OD2 A:ASP223 3.7 16.0 1.0
NE2 A:HIS294 3.8 28.8 1.0
OD2 A:ASP212 4.0 17.9 1.0
CE1 A:HIS294 4.2 31.2 1.0
NE2 A:HIS287 4.2 14.8 1.0
O A:HOH1743 4.2 47.5 1.0
OD1 A:ASP223 4.3 15.6 1.0
CG A:ASP223 4.4 16.2 1.0
OD1 A:ASP212 4.4 15.2 1.0
OE1 A:GLU316 4.5 23.5 1.0
CG A:ASP212 4.6 15.6 1.0
CZ A:PHE181 4.6 19.6 1.0
NE2 A:HIS195 4.7 30.2 1.0
OE2 A:GLU316 4.7 22.7 1.0
CE1 A:PHE181 4.7 20.5 1.0
CE2 A:PHE181 4.8 20.6 1.0
OE2 A:GLU330 4.9 18.7 1.0
OE1 A:GLU330 4.9 16.7 1.0
CD2 A:HIS294 4.9 29.1 1.0
CD2 A:HIS287 5.0 15.2 1.0

Arsenic binding site 2 out of 2 in 1wy2

Go back to Arsenic Binding Sites List in 1wy2
Arsenic binding site 2 out of 2 in the Crystal Structure of the Prolidase From Pyrococcus Horikoshii OT3


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 2 of Crystal Structure of the Prolidase From Pyrococcus Horikoshii OT3 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:As404

b:30.4
occ:1.00
AS B:CAC404 0.0 30.4 1.0
O2 B:CAC404 1.6 27.2 1.0
O1 B:CAC404 1.6 23.6 1.0
C2 B:CAC404 1.9 27.9 1.0
C1 B:CAC404 1.9 29.4 1.0
ZN B:ZN408 3.3 17.6 1.0
ZN B:ZN407 3.3 16.9 1.0
O B:HOH538 3.7 35.4 1.0
NE2 B:HIS294 3.7 30.3 1.0
OD2 B:ASP223 3.8 16.0 1.0
OD2 B:ASP212 3.9 15.2 1.0
O B:HOH548 4.3 37.8 1.0
NE2 B:HIS287 4.3 14.2 1.0
OD1 B:ASP223 4.3 14.4 1.0
CE1 B:HIS294 4.4 30.6 1.0
OE1 B:GLU316 4.4 23.6 1.0
OD1 B:ASP212 4.5 15.0 1.0
CG B:ASP223 4.5 16.7 1.0
CG B:ASP212 4.5 12.7 1.0
OE2 B:GLU316 4.6 19.3 1.0
CZ B:PHE181 4.7 19.1 1.0
CD2 B:HIS294 4.8 28.8 1.0
OE2 B:GLU330 4.8 18.4 1.0
CE1 B:PHE181 4.8 18.9 1.0
OE1 B:GLU330 4.9 16.2 1.0
O B:HOH627 4.9 46.2 1.0
CE2 B:PHE181 4.9 18.8 1.0
CD B:GLU316 4.9 22.3 1.0
CD2 B:HIS287 5.0 17.2 1.0

Reference:

H.Mizutani, N.Kunishima. Crystal Structure of the Prolidase From Pyrococcus Horikoshii OT3 To Be Published.
Page generated: Tue Oct 27 16:47:41 2020

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