Manganese in PDB 3mfv: Crystal Structure of Human Arginase I in Complex with 2- Aminohomohistidine

All present enzymatic activity of Crystal Structure of Human Arginase I in Complex with 2- Aminohomohistidine:
3.5.3.1;

The structure of Crystal Structure of Human Arginase I in Complex with 2- Aminohomohistidine, PDB code: 3mfv was solved by L.Di Costanzo, D.W.Christianson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.90
Space group	P 3
Cell size a, b, c (Å), α, β, γ (°)	90.660, 90.660, 69.707, 90.00, 90.00, 120.00
R / Rfree (%)	14.1 / 19

The binding sites of Manganese atom in the Crystal Structure of Human Arginase I in Complex with 2- Aminohomohistidine (pdb code 3mfv). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 4 binding sites of Manganese where determined in the Crystal Structure of Human Arginase I in Complex with 2- Aminohomohistidine, PDB code: 3mfv:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in the Crystal Structure of Human Arginase I in Complex with 2- Aminohomohistidine


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 Human Arginase I in Complex with 2- Aminohomohistidine within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn614 b:18.9 occ:1.00 OD1 A:ASP124 2.0 14.0 1.0 OD2 A:ASP232 2.2 16.4 1.0 ND1 A:HIS126 2.2 11.7 1.0 OD2 A:ASP234 2.3 14.7 1.0 OD1 A:ASP234 2.3 15.1 1.0 CG A:ASP234 2.7 14.4 1.0 CE1 A:HIS126 2.8 11.2 1.0 N4 A:Z700 2.9 33.4 1.0 CG A:ASP124 3.0 13.8 1.0 CG A:ASP232 3.2 18.1 1.0 C4 A:Z700 3.2 33.6 1.0 OD2 A:ASP124 3.3 14.9 1.0 CG A:HIS126 3.4 13.5 1.0 N3 A:Z700 3.4 34.6 1.0 MN A:MN615 3.5 21.8 1.0 OD1 A:ASP232 3.9 16.2 1.0 N A:ALA125 3.9 12.5 1.0 N A:HIS126 3.9 12.5 1.0 CB A:HIS126 4.0 15.2 1.0 NE2 A:HIS126 4.1 12.2 1.0 N2 A:Z700 4.1 35.9 1.0 CB A:ASP232 4.1 17.7 1.0 CB A:ASP234 4.2 13.2 1.0 OG1 A:THR246 4.3 16.4 1.0 CB A:ASP124 4.3 15.0 1.0 CD2 A:HIS126 4.4 13.2 1.0 C5 A:Z700 4.4 35.2 1.0 CB A:ALA125 4.5 9.3 1.0 CA A:HIS126 4.6 13.2 1.0 CA A:ALA125 4.6 11.1 1.0 C A:ALA125 4.6 11.0 1.0 CA A:ASP124 4.7 13.6 1.0 C A:ASP124 4.7 12.6 1.0 C3 A:Z700 4.8 35.1 1.0 OD1 A:ASP128 4.8 12.3 1.0 O A:HOH400 4.8 11.1 1.0 OD2 A:ASP128 5.0 16.6 1.0 C A:ASP234 5.0 12.6 1.0

Manganese binding site 2 out of 4 in the Crystal Structure of Human Arginase I in Complex with 2- Aminohomohistidine


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 Human Arginase I in Complex with 2- Aminohomohistidine within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn615 b:21.8 occ:1.00 OD2 A:ASP124 2.0 14.9 1.0 OD2 A:ASP128 2.1 16.6 1.0 ND1 A:HIS101 2.3 16.1 1.0 N4 A:Z700 2.4 33.4 1.0 OD2 A:ASP232 2.6 16.4 1.0 CG A:ASP124 3.1 13.8 1.0 CG A:ASP128 3.1 13.4 1.0 CG A:HIS101 3.2 16.9 1.0 CE1 A:HIS101 3.3 16.8 1.0 CB A:HIS101 3.4 17.1 1.0 C4 A:Z700 3.4 33.6 1.0 CG A:ASP232 3.4 18.1 1.0 MN A:MN614 3.5 18.9 1.0 OD1 A:ASP128 3.5 12.3 1.0 OD1 A:ASP124 3.5 14.0 1.0 N2 A:Z700 3.7 35.9 1.0 CB A:ASP232 3.7 17.7 1.0 O A:HIS141 4.2 13.8 1.0 NE1 A:TRP122 4.3 14.4 1.0 CD2 A:HIS101 4.4 17.5 1.0 CB A:ASP124 4.4 15.0 1.0 NE2 A:HIS101 4.4 16.7 1.0 CB A:ASP128 4.4 14.1 1.0 OD1 A:ASP232 4.5 16.2 1.0 OE2 A:GLU277 4.5 16.3 1.0 CZ2 A:TRP122 4.6 13.8 1.0 N3 A:Z700 4.6 34.6 1.0 CG A:GLU277 4.7 14.2 1.0 CE2 A:TRP122 4.8 13.7 1.0 ND1 A:HIS126 4.9 11.7 1.0 CA A:HIS101 4.9 16.1 1.0

Manganese binding site 3 out of 4 in the Crystal Structure of Human Arginase I in Complex with 2- Aminohomohistidine


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Crystal Structure of Human Arginase I in Complex with 2- Aminohomohistidine within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn614 b:20.1 occ:1.00 OD1 B:ASP234 2.1 24.0 1.0 OD2 B:ASP232 2.1 16.7 1.0 ND1 B:HIS126 2.3 18.4 1.0 OD1 B:ASP124 2.3 17.4 1.0 OD2 B:ASP234 2.4 21.5 1.0 CG B:ASP234 2.6 23.2 1.0 N4 B:Z70323 2.7 34.0 1.0 CG B:ASP232 3.0 17.7 1.0 CE1 B:HIS126 3.0 18.6 1.0 C4 B:Z70323 3.1 35.6 1.0 CG B:ASP124 3.1 16.7 1.0 OD2 B:ASP124 3.2 16.0 1.0 N3 B:Z70323 3.3 35.4 1.0 MN B:MN615 3.4 30.4 1.0 CG B:HIS126 3.4 20.5 1.0 OD1 B:ASP232 3.6 16.7 1.0 CB B:HIS126 3.9 17.0 1.0 CB B:ASP232 4.0 18.0 1.0 N2 B:Z70323 4.0 36.2 1.0 CB B:ASP234 4.1 20.9 1.0 N B:HIS126 4.1 16.1 1.0 NE2 B:HIS126 4.2 20.4 1.0 N B:ALA125 4.3 15.9 1.0 C5 B:Z70323 4.4 35.5 1.0 OG1 B:THR246 4.4 23.8 1.0 CD2 B:HIS126 4.4 18.5 1.0 CB B:ASP124 4.5 17.6 1.0 CA B:HIS126 4.6 17.1 1.0 C3 B:Z70323 4.7 35.7 1.0 OD1 B:ASP128 4.7 14.5 1.0 O B:HOH331 4.8 19.8 1.0 OD2 B:ASP128 4.9 13.6 1.0 CB B:ALA125 4.9 15.7 1.0 CA B:ASP124 4.9 15.6 1.0 C B:ALA125 5.0 13.8 1.0 CA B:ASP234 5.0 18.1 1.0 C B:ASP234 5.0 17.7 1.0 CG B:GLU277 5.0 25.6 1.0

Manganese binding site 4 out of 4 in the Crystal Structure of Human Arginase I in Complex with 2- Aminohomohistidine


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Crystal Structure of Human Arginase I in Complex with 2- Aminohomohistidine within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn615 b:30.4 occ:1.00 OD2 B:ASP128 2.1 13.6 1.0 OD2 B:ASP124 2.3 16.0 1.0 ND1 B:HIS101 2.4 21.0 1.0 N4 B:Z70323 2.6 34.0 1.0 OD2 B:ASP232 2.6 16.7 1.0 CG B:ASP128 3.1 15.2 1.0 CG B:HIS101 3.2 22.5 1.0 CB B:HIS101 3.3 21.5 1.0 CG B:ASP124 3.4 16.7 1.0 MN B:MN614 3.4 20.1 1.0 CE1 B:HIS101 3.4 20.0 1.0 OD1 B:ASP128 3.5 14.5 1.0 C4 B:Z70323 3.5 35.6 1.0 CG B:ASP232 3.6 17.7 1.0 N2 B:Z70323 3.8 36.2 1.0 CB B:ASP232 3.8 18.0 1.0 OD1 B:ASP124 3.8 17.4 1.0 O B:HIS141 4.2 25.3 1.0 NE1 B:TRP122 4.3 17.2 1.0 CZ2 B:TRP122 4.3 15.9 1.0 CB B:ASP128 4.4 15.2 1.0 CD2 B:HIS101 4.4 22.8 1.0 NE2 B:HIS101 4.5 20.1 1.0 CB B:ASP124 4.6 17.6 1.0 CE2 B:TRP122 4.7 18.3 1.0 OD1 B:ASP232 4.7 16.7 1.0 CG B:GLU277 4.8 25.6 1.0 N3 B:Z70323 4.8 35.4 1.0 CA B:HIS101 4.8 21.5 1.0 OE2 B:GLU277 4.9 30.0 1.0

M.Ilies, L.Di Costanzo, M.L.North, J.A.Scott, D.W.Christianson. 2-Aminoimidazole Amino Acids As Inhibitors of the Binuclear Manganese Metalloenzyme Human Arginase I. J.Med.Chem. V. 53 4266 2010.
ISSN: ISSN 0022-2623
PubMed: 20441173
DOI: 10.1021/JM100306A