Arsenic in PDB 7oi1: Crystal Structure of Synechocystis Sp PCC6803 Guanidinium Hydrolase

All present enzymatic activity of Crystal Structure of Synechocystis Sp PCC6803 Guanidinium Hydrolase:
3.5.3.11;

The structure of Crystal Structure of Synechocystis Sp PCC6803 Guanidinium Hydrolase, PDB code: 7oi1 was solved by J.R.Fleming, O.M.Mayans, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.15 / 1.90
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	102.36, 140.21, 86.85, 90, 119.75, 90
R / Rfree (%)	17.3 / 20.8

The structure of Crystal Structure of Synechocystis Sp PCC6803 Guanidinium Hydrolase also contains other interesting chemical elements:

Nickel	(Ni)	6 atoms
Chlorine	(Cl)	2 atoms

The binding sites of Arsenic atom in the Crystal Structure of Synechocystis Sp PCC6803 Guanidinium Hydrolase (pdb code 7oi1). This binding sites where shown within 5.0 Angstroms radius around Arsenic atom.
In total 3 binding sites of Arsenic where determined in the Crystal Structure of Synechocystis Sp PCC6803 Guanidinium Hydrolase, PDB code: 7oi1:
Jump to Arsenic binding site number: 1; 2; 3;

Arsenic binding site 1 out of 3 in the Crystal Structure of Synechocystis Sp PCC6803 Guanidinium Hydrolase


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 Synechocystis Sp PCC6803 Guanidinium Hydrolase within 5.0Å range: probe atom residue distance (Å) B Occ A:As404 b:49.4 occ:0.83 AS A:CAC404 0.0 49.4 0.8 O2 A:CAC404 1.7 51.5 0.8 O1 A:CAC404 1.8 43.0 0.8 C2 A:CAC404 1.9 41.9 0.8 C1 A:CAC404 2.0 41.9 0.8 NI A:NI403 2.9 45.3 0.9 NI A:NI402 3.0 43.2 0.9 OD2 A:ASP291 3.3 40.0 1.0 OD1 A:ASP203 3.4 45.5 1.0 ND1 A:HIS201 3.8 41.1 1.0 OD2 A:ASP203 4.0 42.5 1.0 ND1 A:HIS214 4.0 43.1 1.0 O A:HIS214 4.0 42.5 1.0 OE2 A:GLU336 4.0 39.5 1.0 CG A:ASP203 4.1 44.1 1.0 OD2 A:ASP293 4.1 42.5 1.0 CE3 A:TRP305 4.1 46.3 1.0 CE1 A:HIS214 4.3 41.6 1.0 CB A:HIS201 4.3 41.8 1.0 CD2 A:TRP305 4.3 45.5 1.0 CG A:HIS214 4.3 42.2 1.0 CG A:HIS201 4.3 43.5 1.0 OD1 A:ASP199 4.5 37.4 1.0 CZ3 A:TRP305 4.5 46.2 1.0 CG A:ASP291 4.6 45.0 1.0 OD2 A:ASP199 4.6 49.2 1.0 CE1 A:HIS201 4.7 44.2 1.0 CG A:TRP305 4.7 43.0 1.0 CB A:HIS174 4.7 41.1 1.0 NE2 A:HIS214 4.7 41.2 1.0 CD A:GLU336 4.7 45.4 1.0 C A:HIS214 4.8 42.5 1.0 CD2 A:HIS214 4.8 39.8 1.0 CB A:HIS214 4.8 38.7 1.0 ND1 A:HIS174 4.8 41.1 1.0 CE2 A:TRP305 4.8 48.0 1.0 CG A:GLU336 5.0 38.1 1.0 CG A:ASP199 5.0 40.6 1.0 O A:HOH543 5.0 39.4 1.0 CH2 A:TRP305 5.0 46.2 1.0 CB A:TRP305 5.0 41.4 1.0

Arsenic binding site 2 out of 3 in the Crystal Structure of Synechocystis Sp PCC6803 Guanidinium Hydrolase


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 Synechocystis Sp PCC6803 Guanidinium Hydrolase within 5.0Å range: probe atom residue distance (Å) B Occ B:As403 b:53.9 occ:0.80 AS B:CAC403 0.0 53.9 0.8 O2 B:CAC403 1.7 51.4 0.8 O1 B:CAC403 1.8 48.3 0.8 C2 B:CAC403 1.9 44.5 0.8 C1 B:CAC403 2.0 41.5 0.8 NI B:NI401 2.9 47.7 0.9 NI B:NI402 3.2 47.8 0.8 OD1 B:ASP203 3.4 44.3 1.0 OD2 B:ASP291 3.5 41.6 1.0 ND1 B:HIS201 3.9 45.3 1.0 OD2 B:ASP203 3.9 45.2 1.0 ND1 B:HIS214 3.9 47.4 1.0 CG B:ASP203 4.1 42.4 1.0 O B:HIS214 4.1 43.5 1.0 OE2 B:GLU336 4.2 41.0 1.0 CE1 B:HIS214 4.2 40.6 1.0 OD2 B:ASP293 4.2 41.0 1.0 CE3 B:TRP305 4.2 48.1 1.0 CG B:HIS214 4.2 45.5 1.0 CB B:HIS201 4.3 45.6 1.0 CD2 B:TRP305 4.4 46.0 1.0 CG B:HIS201 4.4 45.3 1.0 OD1 B:ASP199 4.6 41.8 1.0 CZ3 B:TRP305 4.6 48.2 1.0 CG B:ASP291 4.7 41.7 1.0 NE2 B:HIS214 4.7 39.0 1.0 CD B:GLU336 4.7 42.1 1.0 CB B:HIS174 4.7 42.8 1.0 CD2 B:HIS214 4.7 43.5 1.0 OD2 B:ASP199 4.7 44.3 1.0 CB B:HIS214 4.7 38.8 1.0 CG B:TRP305 4.7 48.1 1.0 C B:HIS214 4.7 44.4 1.0 CE1 B:HIS201 4.8 45.5 1.0 CE2 B:TRP305 4.9 46.7 1.0 CG B:GLU336 4.9 36.4 1.0 ND1 B:HIS174 4.9 41.4 1.0 CB B:TRP305 5.0 44.4 1.0

Arsenic binding site 3 out of 3 in the Crystal Structure of Synechocystis Sp PCC6803 Guanidinium Hydrolase


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 3 of Crystal Structure of Synechocystis Sp PCC6803 Guanidinium Hydrolase within 5.0Å range: probe atom residue distance (Å) B Occ C:As404 b:54.5 occ:0.85 AS C:CAC404 0.0 54.5 0.8 O2 C:CAC404 1.7 48.8 0.8 O1 C:CAC404 1.7 45.0 0.8 C2 C:CAC404 1.9 40.2 0.8 C1 C:CAC404 2.0 40.9 0.8 NI C:NI403 2.9 49.3 0.9 NI C:NI402 3.2 49.6 0.9 OD1 C:ASP203 3.3 42.1 1.0 OD2 C:ASP291 3.4 42.2 1.0 OD2 C:ASP203 3.9 49.8 1.0 ND1 C:HIS201 4.0 43.6 1.0 CG C:ASP203 4.0 44.6 1.0 ND1 C:HIS214 4.0 43.6 1.0 OE2 C:GLU336 4.1 43.4 1.0 O C:HIS214 4.1 44.3 1.0 CE3 C:TRP305 4.2 50.6 1.0 CG C:HIS214 4.2 44.9 1.0 OD2 C:ASP293 4.3 42.2 1.0 CB C:HIS201 4.3 44.1 1.0 CE1 C:HIS214 4.3 41.9 1.0 CD2 C:TRP305 4.4 48.4 1.0 CG C:HIS201 4.5 44.7 1.0 CZ3 C:TRP305 4.5 49.3 1.0 OD1 C:ASP199 4.6 39.1 1.0 OD2 C:ASP199 4.6 43.6 1.0 CG C:ASP291 4.6 42.9 1.0 C C:HIS214 4.6 42.7 1.0 CB C:HIS214 4.6 41.3 1.0 CD2 C:HIS214 4.7 44.6 1.0 CB C:HIS174 4.7 41.5 1.0 NE2 C:HIS214 4.7 45.4 1.0 CD C:GLU336 4.7 45.4 1.0 CG C:TRP305 4.8 45.9 1.0 CE2 C:TRP305 4.9 44.0 1.0 ND1 C:HIS174 4.9 43.5 1.0 CE1 C:HIS201 4.9 38.7 1.0 CG C:GLU336 5.0 38.9 1.0

D.Funck, M.Sinn, J.R.Fleming, M.Stanoppi, J.Dietrich, R.Lopez-Igual, O.Mayans, J.S.Hartig. Guanidine Hydrolase Is A Novel NI2+-Dependent Enzyme From the Arginase Family Nature 2021.
ISSN: ESSN 1476-4687