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Arsenic in PDB 3s2s: The Crystal Structure of Pyrazinamidase/Nicotinamidase From Streptococcus Mutans UA159

Enzymatic activity of The Crystal Structure of Pyrazinamidase/Nicotinamidase From Streptococcus Mutans UA159

All present enzymatic activity of The Crystal Structure of Pyrazinamidase/Nicotinamidase From Streptococcus Mutans UA159:
3.5.1.19;

Protein crystallography data

The structure of The Crystal Structure of Pyrazinamidase/Nicotinamidase From Streptococcus Mutans UA159, PDB code: 3s2s was solved by X.-D.Su, X.Liu, H.Zhang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.98 / 1.70
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 76.490, 80.120, 130.960, 90.00, 90.00, 90.00
R / Rfree (%) 16 / 19.1

Other elements in 3s2s:

The structure of The Crystal Structure of Pyrazinamidase/Nicotinamidase From Streptococcus Mutans UA159 also contains other interesting chemical elements:

Zinc (Zn) 4 atoms

Arsenic Binding Sites:

The binding sites of Arsenic atom in the The Crystal Structure of Pyrazinamidase/Nicotinamidase From Streptococcus Mutans UA159 (pdb code 3s2s). This binding sites where shown within 5.0 Angstroms radius around Arsenic atom.
In total 4 binding sites of Arsenic where determined in the The Crystal Structure of Pyrazinamidase/Nicotinamidase From Streptococcus Mutans UA159, PDB code: 3s2s:
Jump to Arsenic binding site number: 1; 2; 3; 4;

Arsenic binding site 1 out of 4 in 3s2s

Go back to Arsenic Binding Sites List in 3s2s
Arsenic binding site 1 out of 4 in the The Crystal Structure of Pyrazinamidase/Nicotinamidase From Streptococcus Mutans UA159


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 1 of The Crystal Structure of Pyrazinamidase/Nicotinamidase From Streptococcus Mutans UA159 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:As185

b:24.6
occ:0.80
 AS A:CAD185 0.0 24.6 0.8
O1 A:CAD185 1.6 32.6 1.0
C1 A:CAD185 1.9 19.9 1.0
C2 A:CAD185 2.0 26.5 1.0
SG A:CYS136 2.3 20.9 1.0
CB A:CYS136 3.2 14.7 1.0
N A:CYS136 3.6 16.5 1.0
N A:LEU132 3.8 18.3 1.0
OD2 A:ASP9 3.9 29.6 1.0
O A:VAL131 4.0 17.5 1.0
CA A:CYS136 4.0 17.1 1.0
CG2 A:ILE135 4.1 22.8 1.0
CB A:ILE135 4.2 17.9 1.0
O A:HOH401 4.3 35.8 1.0
C A:VAL131 4.3 17.2 1.0
CE1 A:PHE14 4.4 30.7 1.0
CZ A:PHE14 4.5 23.7 1.0
CG A:LEU132 4.6 32.3 1.0
CB A:LEU132 4.7 25.3 1.0
C A:ILE135 4.7 16.9 1.0
CD1 A:TYR106 4.8 20.4 1.0
CA A:LEU132 4.8 20.0 1.0
CG A:ASP9 4.8 25.3 1.0
CD1 A:PHE14 5.0 31.8 1.0

Arsenic binding site 2 out of 4 in 3s2s

Go back to Arsenic Binding Sites List in 3s2s
Arsenic binding site 2 out of 4 in the The Crystal Structure of Pyrazinamidase/Nicotinamidase From Streptococcus Mutans UA159


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 2 of The Crystal Structure of Pyrazinamidase/Nicotinamidase From Streptococcus Mutans UA159 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:As185

b:25.0
occ:0.80
 AS B:CAD185 0.0 25.0 0.8
O1 B:CAD185 1.6 36.7 1.0
C2 B:CAD185 1.9 23.3 1.0
C1 B:CAD185 2.0 19.1 1.0
SG B:CYS136 2.3 22.5 1.0
CB B:CYS136 3.2 20.1 1.0
N B:CYS136 3.7 17.9 1.0
O B:HOH306 3.7 29.8 1.0
N B:LEU132 3.8 21.6 1.0
OD2 B:ASP9 3.8 30.4 1.0
O B:VAL131 3.9 22.0 1.0
CA B:CYS136 4.0 19.7 1.0
CG2 B:ILE135 4.2 21.5 1.0
C B:VAL131 4.3 22.4 1.0
CB B:ILE135 4.3 20.8 1.0
CZ B:PHE14 4.5 30.2 1.0
CD1 B:TYR106 4.5 19.0 1.0
CG B:LEU132 4.6 32.2 1.0
CE1 B:PHE14 4.7 35.0 1.0
CD1 B:LEU132 4.7 34.3 1.0
CB B:LEU132 4.7 27.2 1.0
C B:ILE135 4.8 17.9 1.0
CG B:ASP9 4.8 27.1 1.0
CE2 B:PHE14 4.9 30.2 1.0
CA B:LEU132 4.9 22.4 1.0
CB B:ASP9 5.0 19.9 1.0

Arsenic binding site 3 out of 4 in 3s2s

Go back to Arsenic Binding Sites List in 3s2s
Arsenic binding site 3 out of 4 in the The Crystal Structure of Pyrazinamidase/Nicotinamidase From Streptococcus Mutans UA159


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 3 of The Crystal Structure of Pyrazinamidase/Nicotinamidase From Streptococcus Mutans UA159 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:As185

b:23.7
occ:0.80
 AS C:CAD185 0.0 23.7 0.8
O1 C:CAD185 1.7 32.2 1.0
C1 C:CAD185 1.9 26.3 1.0
C2 C:CAD185 2.0 16.4 1.0
SG C:CYS136 2.3 22.5 1.0
CB C:CYS136 3.3 20.6 1.0
N C:CYS136 3.7 19.6 1.0
O C:HOH430 3.7 30.6 1.0
N C:LEU132 3.8 21.6 1.0
OD2 C:ASP9 3.9 29.0 1.0
O C:VAL131 4.0 21.0 1.0
CA C:CYS136 4.1 18.9 1.0
CG2 C:ILE135 4.2 21.8 1.0
CB C:ILE135 4.3 20.7 1.0
C C:VAL131 4.3 22.4 1.0
CZ C:PHE14 4.5 27.6 1.0
CD1 C:TYR106 4.6 19.8 1.0
CG C:LEU132 4.6 25.6 1.0
CE1 C:PHE14 4.6 31.7 1.0
CB C:LEU132 4.7 20.8 1.0
C C:ILE135 4.8 20.5 1.0
CG C:ASP9 4.8 27.7 1.0
CA C:LEU132 4.9 21.3 1.0
CE2 C:PHE14 4.9 24.6 1.0
CD1 C:LEU132 4.9 32.1 1.0
CB C:ASP9 5.0 20.0 1.0

Arsenic binding site 4 out of 4 in 3s2s

Go back to Arsenic Binding Sites List in 3s2s
Arsenic binding site 4 out of 4 in the The Crystal Structure of Pyrazinamidase/Nicotinamidase From Streptococcus Mutans UA159


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 4 of The Crystal Structure of Pyrazinamidase/Nicotinamidase From Streptococcus Mutans UA159 within 5.0Å range:
probe atom residue distance (Å) B Occ
D:As185

b:23.8
occ:0.80
 AS D:CAD185 0.0 23.8 0.8
O1 D:CAD185 1.6 38.1 1.0
C2 D:CAD185 1.9 17.8 1.0
C1 D:CAD185 2.0 28.1 1.0
SG D:CYS136 2.3 23.5 1.0
CB D:CYS136 3.2 22.4 1.0
N D:CYS136 3.6 16.6 1.0
O D:HOH315 3.8 29.6 1.0
N D:LEU132 3.8 23.4 1.0
O D:VAL131 3.9 23.1 1.0
OD2 D:ASP9 3.9 27.1 1.0
CA D:CYS136 4.0 17.9 1.0
CG2 D:ILE135 4.1 21.8 1.0
C D:VAL131 4.3 23.2 1.0
CB D:ILE135 4.3 22.1 1.0
CD1 D:TYR106 4.5 19.5 1.0
CZ D:PHE14 4.5 30.3 1.0
CG D:LEU132 4.7 27.1 1.0
CE2 D:PHE14 4.7 28.5 1.0
C D:ILE135 4.8 18.5 1.0
CD1 D:LEU132 4.8 32.2 1.0
CB D:LEU132 4.8 26.4 1.0
CG D:ASP9 4.9 26.8 1.0
CE1 D:PHE14 4.9 29.4 1.0
CA D:LEU132 4.9 21.9 1.0
CB D:ASP9 5.0 23.6 1.0

Reference:

X.Liu, H.Zhang, X.J.Wang, L.F.Li, X.-D.Su. Get Phases From Arsenic Anomalous Scattering: De Novo Sad Phasing of Two Protein Structures Crystallized in Cacodylate Buffer Plos One V. 6 24227 2011.
ISSN: ESSN 1932-6203
PubMed: 21912678
DOI: 10.1371/JOURNAL.PONE.0024227
Page generated: Wed Jul 10 11:53:39 2024

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