Manganese in PDB 3gmz: Crystal of Human Arginase in Complex with L-Ornithine. Resolution 1.43 A.

All present enzymatic activity of Crystal of Human Arginase in Complex with L-Ornithine. Resolution 1.43 A.:
3.5.3.1;

The structure of Crystal of Human Arginase in Complex with L-Ornithine. Resolution 1.43 A., PDB code: 3gmz 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 / 1.43
Space group	P 3
Cell size a, b, c (Å), α, β, γ (°)	90.392, 90.392, 69.422, 90.00, 90.00, 120.00
R / Rfree (%)	14.7 / 18.5

The binding sites of Manganese atom in the Crystal of Human Arginase in Complex with L-Ornithine. Resolution 1.43 A. (pdb code 3gmz). 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 of Human Arginase in Complex with L-Ornithine. Resolution 1.43 A., PDB code: 3gmz:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in the Crystal of Human Arginase in Complex with L-Ornithine. Resolution 1.43 A.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal of Human Arginase in Complex with L-Ornithine. Resolution 1.43 A. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn536 b:12.5 occ:1.00 O A:HOH527 2.2 17.2 1.0 OD1 A:ASP124 2.2 13.5 1.0 OD2 A:ASP232 2.3 13.1 1.0 OD1 A:ASP234 2.3 12.9 1.0 ND1 A:HIS126 2.4 11.9 1.0 OD2 A:ASP234 2.4 12.2 1.0 CG A:ASP234 2.7 12.3 1.0 O A:HOH473 3.0 15.1 1.0 CG A:ASP232 3.2 14.4 1.0 CG A:ASP124 3.2 13.8 1.0 CE1 A:HIS126 3.2 10.9 1.0 MN A:MN537 3.3 12.9 1.0 OD2 A:ASP124 3.5 13.8 1.0 CG A:HIS126 3.5 11.1 1.0 OD1 A:ASP232 3.7 14.8 1.0 CB A:HIS126 3.9 11.5 1.0 OG1 A:THR246 3.9 13.4 1.0 N A:HIS126 4.0 10.7 1.0 N A:ALA125 4.1 11.2 1.0 CB A:ASP232 4.1 13.9 1.0 CB A:ASP234 4.2 12.2 1.0 O A:HOH528 4.2 19.4 1.0 NE A:ORN551 4.3 12.6 1.0 NE2 A:HIS126 4.4 12.6 1.0 CB A:ASP124 4.5 13.0 1.0 CD2 A:HIS126 4.5 11.1 1.0 CA A:HIS126 4.5 11.2 1.0 CD A:ORN551 4.6 12.8 1.0 O A:HOH403 4.6 11.2 1.0 CB A:ALA125 4.6 11.2 1.0 OD1 A:ASP128 4.7 11.0 1.0 CA A:ALA125 4.8 11.1 1.0 C A:ALA125 4.8 10.2 1.0 OD2 A:ASP128 4.8 12.5 1.0 CA A:ASP124 4.9 12.1 1.0 O A:THR246 4.9 13.0 1.0 C A:ASP124 5.0 11.2 1.0

Manganese binding site 2 out of 4 in the Crystal of Human Arginase in Complex with L-Ornithine. Resolution 1.43 A.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal of Human Arginase in Complex with L-Ornithine. Resolution 1.43 A. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn537 b:12.9 occ:1.00 OD2 A:ASP124 2.1 13.8 1.0 OD2 A:ASP128 2.2 12.5 1.0 ND1 A:HIS101 2.3 12.0 1.0 O A:HOH527 2.3 17.2 1.0 OD2 A:ASP232 2.3 13.1 1.0 O A:HOH528 2.5 19.4 1.0 CG A:ASP124 3.1 13.8 1.0 CG A:ASP128 3.2 10.0 1.0 CG A:HIS101 3.2 13.2 1.0 CE1 A:HIS101 3.3 12.3 1.0 CG A:ASP232 3.3 14.4 1.0 MN A:MN536 3.3 12.5 1.0 OD1 A:ASP124 3.4 13.5 1.0 CB A:HIS101 3.5 13.3 1.0 OD1 A:ASP128 3.6 11.0 1.0 CB A:ASP232 3.6 13.9 1.0 O A:HOH473 4.0 15.1 1.0 NE A:ORN551 4.1 12.6 1.0 NE1 A:TRP122 4.3 13.5 1.0 NE2 A:HIS101 4.4 12.3 1.0 CD2 A:HIS101 4.4 13.1 1.0 OD1 A:ASP232 4.4 14.8 1.0 CB A:ASP124 4.4 13.0 1.0 O A:HIS141 4.5 12.5 1.0 CB A:ASP128 4.5 11.9 1.0 CZ2 A:TRP122 4.6 14.3 1.0 OE2 A:GLU277 4.6 12.5 1.0 CG A:GLU277 4.6 14.1 1.0 CE2 A:TRP122 4.8 13.7 1.0 CA A:ASP232 4.9 12.9 1.0 CA A:HIS101 5.0 13.8 1.0

Manganese binding site 3 out of 4 in the Crystal of Human Arginase in Complex with L-Ornithine. Resolution 1.43 A.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Crystal of Human Arginase in Complex with L-Ornithine. Resolution 1.43 A. within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn536 b:15.1 occ:1.00 OD1 B:ASP234 2.2 15.5 1.0 O B:HOH501 2.2 15.9 1.0 OD1 B:ASP124 2.3 13.1 1.0 ND1 B:HIS126 2.4 14.7 1.0 OD2 B:ASP232 2.4 16.8 1.0 OD2 B:ASP234 2.5 13.1 1.0 CG B:ASP234 2.6 17.0 1.0 O B:HOH499 3.0 22.0 1.0 CE1 B:HIS126 3.1 14.7 1.0 CG B:ASP232 3.2 14.8 1.0 CG B:ASP124 3.2 11.9 1.0 MN B:MN537 3.4 15.9 1.0 CG B:HIS126 3.5 16.0 1.0 OD2 B:ASP124 3.5 14.4 1.0 OD1 B:ASP232 3.6 13.4 1.0 CB B:HIS126 3.9 13.7 1.0 OG1 B:THR246 3.9 18.4 1.0 O B:HOH500 4.0 15.4 1.0 N B:HIS126 4.0 12.4 1.0 CB B:ASP232 4.2 14.4 1.0 CB B:ASP234 4.2 15.0 1.0 N B:ALA125 4.2 12.3 1.0 NE B:ORN552 4.3 13.5 1.0 NE2 B:HIS126 4.3 15.3 1.0 CD2 B:HIS126 4.5 16.2 1.0 CD B:ORN552 4.5 14.1 1.0 O B:HOH342 4.6 14.2 1.0 CA B:HIS126 4.6 14.1 1.0 CB B:ASP124 4.6 12.9 1.0 OD1 B:ASP128 4.6 14.9 1.0 CB B:ALA125 4.7 11.9 1.0 O B:THR246 4.8 17.5 1.0 C B:ALA125 4.9 11.5 1.0 CA B:ALA125 4.9 11.5 1.0 OD2 B:ASP128 4.9 13.7 1.0 CA B:ASP124 4.9 13.0 1.0

Manganese binding site 4 out of 4 in the Crystal of Human Arginase in Complex with L-Ornithine. Resolution 1.43 A.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Crystal of Human Arginase in Complex with L-Ornithine. Resolution 1.43 A. within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn537 b:15.9 occ:1.00 OD2 B:ASP128 2.2 13.7 1.0 ND1 B:HIS101 2.2 16.8 1.0 OD2 B:ASP124 2.2 14.4 1.0 O B:HOH501 2.3 15.9 1.0 OD2 B:ASP232 2.3 16.8 1.0 O B:HOH500 2.4 15.4 1.0 CG B:HIS101 3.2 16.1 1.0 CG B:ASP128 3.2 13.7 1.0 CE1 B:HIS101 3.2 15.7 1.0 CG B:ASP124 3.2 11.9 1.0 CG B:ASP232 3.3 14.8 1.0 MN B:MN536 3.4 15.1 1.0 CB B:HIS101 3.4 16.8 1.0 OD1 B:ASP128 3.5 14.9 1.0 OD1 B:ASP124 3.6 13.1 1.0 CB B:ASP232 3.6 14.4 1.0 O B:HOH499 4.1 22.0 1.0 NE B:ORN552 4.1 13.5 1.0 CD2 B:HIS101 4.3 17.9 1.0 NE2 B:HIS101 4.3 16.2 1.0 NE1 B:TRP122 4.3 15.8 1.0 OD1 B:ASP232 4.4 13.4 1.0 O B:HIS141 4.5 18.0 1.0 CB B:ASP128 4.5 12.8 1.0 CZ2 B:TRP122 4.5 16.8 1.0 CG B:GLU277 4.5 19.5 1.0 CB B:ASP124 4.6 12.9 1.0 OE2 B:GLU277 4.6 18.1 1.0 CE2 B:TRP122 4.8 17.3 1.0 CA B:ASP232 4.9 13.7 1.0 CA B:HIS101 4.9 16.4 1.0

M.Ilies, L.Di Costanzo, D.P.Dowling, K.J.Thorn, D.W.Christianson. Binding of Alpha,Alpha-Disubstituted Amino Acids to Arginase Suggests New Avenues For Inhibitor Design J.Med.Chem. V. 54 5432 2011.
ISSN: ISSN 0022-2623
PubMed: 21728378
DOI: 10.1021/JM200443B