Manganese in PDB 4rhl: Crystal Structure of T. Brucei Arginase-Like Protein Triple Mutant S149D/R151H/S226D Bound with MN2+

All present enzymatic activity of Crystal Structure of T. Brucei Arginase-Like Protein Triple Mutant S149D/R151H/S226D Bound with MN2+:
3.5.3.1;

The structure of Crystal Structure of T. Brucei Arginase-Like Protein Triple Mutant S149D/R151H/S226D Bound with MN2+, PDB code: 4rhl was solved by Y.Hai, M.P.Barrett, D.W.Christianson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.61 / 3.10
Space group	P 3 2 1
Cell size a, b, c (Å), α, β, γ (°)	135.582, 135.582, 86.680, 90.00, 90.00, 120.00
R / Rfree (%)	21.5 / 27.4

The binding sites of Manganese atom in the Crystal Structure of T. Brucei Arginase-Like Protein Triple Mutant S149D/R151H/S226D Bound with MN2+ (pdb code 4rhl). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Crystal Structure of T. Brucei Arginase-Like Protein Triple Mutant S149D/R151H/S226D Bound with MN2+, PDB code: 4rhl:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Crystal Structure of T. Brucei Arginase-Like Protein Triple Mutant S149D/R151H/S226D Bound with MN2+


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of T. Brucei Arginase-Like Protein Triple Mutant S149D/R151H/S226D Bound with MN2+ within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn400 b:38.8 occ:1.00 OD2 A:ASP226 2.0 28.7 1.0 OD1 A:ASP149 2.1 32.6 1.0 OD2 A:ASP224 2.1 31.5 1.0 ND1 A:HIS151 2.3 25.9 1.0 O A:HOH515 2.4 29.0 1.0 CG A:ASP226 2.7 31.2 1.0 OD1 A:ASP226 2.7 33.2 1.0 CG A:ASP149 2.9 33.1 1.0 CG A:ASP224 3.1 31.0 1.0 OD2 A:ASP149 3.1 36.5 1.0 CE1 A:HIS151 3.2 27.4 1.0 CG A:HIS151 3.4 28.1 1.0 CB A:HIS151 3.8 33.5 1.0 N A:HIS151 3.9 29.9 1.0 OD1 A:ASP224 3.9 34.6 1.0 CB A:ASP224 4.0 30.0 1.0 N A:ALA150 4.1 30.3 1.0 CB A:ASP226 4.2 29.7 1.0 O A:HOH509 4.3 30.9 1.0 CB A:ASP149 4.3 28.4 1.0 NE2 A:HIS151 4.4 29.1 1.0 CA A:HIS151 4.4 32.5 1.0 CD2 A:HIS151 4.5 28.4 1.0 OG A:SER153 4.6 39.3 1.0 O A:HIS151 4.7 37.3 1.0 CA A:ASP149 4.7 29.8 1.0 C A:ALA150 4.7 28.7 1.0 CA A:ALA150 4.8 28.6 1.0 C A:ASP149 4.9 30.2 1.0 CB A:ALA150 4.9 29.8 1.0

Manganese binding site 2 out of 2 in the Crystal Structure of T. Brucei Arginase-Like Protein Triple Mutant S149D/R151H/S226D Bound with MN2+


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of T. Brucei Arginase-Like Protein Triple Mutant S149D/R151H/S226D Bound with MN2+ within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn401 b:45.0 occ:1.00 OD2 B:ASP224 1.9 32.8 1.0 OD2 B:ASP226 2.0 33.8 1.0 OD1 B:ASP149 2.2 37.6 1.0 ND1 B:HIS151 2.5 30.9 1.0 OD1 B:ASP226 2.6 33.6 1.0 CG B:ASP226 2.7 32.4 1.0 CG B:ASP224 3.0 32.6 1.0 CG B:ASP149 3.0 36.8 1.0 OD2 B:ASP149 3.2 42.6 1.0 CE1 B:HIS151 3.3 32.1 1.0 CG B:HIS151 3.6 31.9 1.0 OD1 B:ASP224 3.8 33.5 1.0 CB B:ASP224 3.9 33.7 1.0 CB B:HIS151 3.9 37.7 1.0 N B:HIS151 4.0 33.3 1.0 CB B:ASP226 4.1 31.0 1.0 N B:ALA150 4.2 30.5 1.0 O B:HOH516 4.4 26.1 1.0 OG B:SER153 4.4 42.2 1.0 CB B:ASP149 4.4 31.9 1.0 NE2 B:HIS151 4.5 33.4 1.0 CA B:HIS151 4.6 34.8 1.0 CD2 B:HIS151 4.6 31.1 1.0 CA B:ASP149 4.8 31.6 1.0 O B:HIS151 4.8 36.7 1.0 C B:ALA150 4.9 32.4 1.0 CA B:ALA150 4.9 31.6 1.0 CB B:ALA150 4.9 31.7 1.0 C B:ASP149 4.9 30.4 1.0

Y.Hai, E.J.Kerkhoven, M.P.Barrett, D.W.Christianson. Crystal Structure of An Arginase-Like Protein From Trypanosoma Brucei That Evolved Without A Binuclear Manganese Cluster. Biochemistry V. 54 458 2015.
ISSN: ISSN 0006-2960
PubMed: 25536859
DOI: 10.1021/BI501366A