Manganese in PDB 4ie1: Crystal Structure of Human Arginase-1 Complexed with Inhibitor 1H

All present enzymatic activity of Crystal Structure of Human Arginase-1 Complexed with Inhibitor 1H:
3.5.3.1;

The structure of Crystal Structure of Human Arginase-1 Complexed with Inhibitor 1H, PDB code: 4ie1 was solved by A.Cousido-Siah, A.Mitschler, F.X.Ruiz, P.Beckett, M.C.Van Zandt, M.K.Ji, D.Whitehouse, T.Ryder, E.Jagdmann, M.Andreoli, A.Mazur, M.Padmanilayam, H.Schroeter, A.Golebiowski, A.Podjarny, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	21.64 / 2.00
Space group	P 3
Cell size a, b, c (Å), α, β, γ (°)	90.074, 90.074, 69.272, 90.00, 90.00, 120.00
R / Rfree (%)	10.6 / 12.7

The binding sites of Manganese atom in the Crystal Structure of Human Arginase-1 Complexed with Inhibitor 1H (pdb code 4ie1). 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-1 Complexed with Inhibitor 1H, PDB code: 4ie1:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in the Crystal Structure of Human Arginase-1 Complexed with Inhibitor 1H


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-1 Complexed with Inhibitor 1H within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn402 b:18.9 occ:1.00 OD2 A:ASP234 2.0 14.4 1.0 O13 A:1EC401 2.1 16.3 1.0 ND1 A:HIS126 2.2 14.1 1.0 OD1 A:ASP124 2.2 14.2 1.0 OD2 A:ASP232 2.3 15.2 1.0 OD1 A:ASP234 2.5 13.2 1.0 CG A:ASP234 2.6 14.2 1.0 O23 A:1EC401 2.9 16.1 1.0 CE1 A:HIS126 3.0 14.4 1.0 CG A:ASP124 3.1 14.7 1.0 B10 A:1EC401 3.2 18.1 1.0 CG A:ASP232 3.3 16.4 1.0 MN A:MN403 3.3 20.1 1.0 CG A:HIS126 3.3 14.5 1.0 OD2 A:ASP124 3.4 14.5 1.0 CB A:HIS126 3.8 13.5 1.0 OD1 A:ASP232 3.8 16.7 1.0 N A:HIS126 3.9 13.8 1.0 O11 A:1EC401 3.9 20.4 1.0 OG1 A:THR246 4.0 22.1 1.0 N A:ALA125 4.1 14.3 1.0 CB A:ASP234 4.1 13.1 1.0 NE2 A:HIS126 4.2 13.2 1.0 CB A:ASP232 4.2 15.8 1.0 C9 A:1EC401 4.4 17.3 1.0 CD2 A:HIS126 4.4 13.6 1.0 OD2 A:ASP128 4.4 15.5 1.0 C8 A:1EC401 4.5 20.1 1.0 CA A:HIS126 4.5 14.6 1.0 CB A:ASP124 4.6 13.9 1.0 O A:HOH515 4.6 18.6 1.0 CB A:ALA125 4.6 12.8 1.0 CA A:ALA125 4.7 13.9 1.0 C A:ALA125 4.7 14.1 1.0 CA A:ASP124 4.9 13.9 1.0 OD1 A:ASP128 4.9 14.9 1.0 C A:ASP124 4.9 13.6 1.0 O A:THR246 5.0 20.4 1.0

Manganese binding site 2 out of 4 in the Crystal Structure of Human Arginase-1 Complexed with Inhibitor 1H


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-1 Complexed with Inhibitor 1H within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn403 b:20.1 occ:1.00 OD2 A:ASP124 2.1 14.5 1.0 OD1 A:ASP128 2.2 14.9 1.0 O11 A:1EC401 2.2 20.4 1.0 OD2 A:ASP232 2.2 15.2 1.0 O13 A:1EC401 2.3 16.3 1.0 ND1 A:HIS101 2.3 16.2 1.0 B10 A:1EC401 2.8 18.1 1.0 CG A:ASP128 3.1 13.5 1.0 CG A:ASP124 3.1 14.7 1.0 CG A:ASP232 3.2 16.4 1.0 CG A:HIS101 3.2 15.4 1.0 OD2 A:ASP128 3.3 15.5 1.0 CE1 A:HIS101 3.3 14.2 1.0 MN A:MN402 3.3 18.9 1.0 OD1 A:ASP124 3.5 14.2 1.0 CB A:HIS101 3.5 17.5 1.0 CB A:ASP232 3.6 15.8 1.0 O23 A:1EC401 3.6 16.1 1.0 C9 A:1EC401 4.2 17.3 1.0 OD1 A:ASP232 4.3 16.7 1.0 O A:HIS141 4.4 16.6 1.0 NE2 A:HIS101 4.4 16.3 1.0 CD2 A:HIS101 4.4 15.6 1.0 NE1 A:TRP122 4.4 14.4 1.0 CB A:ASP124 4.5 13.9 1.0 CB A:ASP128 4.5 14.4 1.0 CZ2 A:TRP122 4.7 12.9 1.0 OD2 A:ASP234 4.7 14.4 1.0 CG A:GLU277 4.9 15.4 1.0 CE2 A:TRP122 4.9 12.3 1.0 CA A:ASP232 4.9 17.0 1.0 ND1 A:HIS126 4.9 14.1 1.0 OE2 A:GLU277 4.9 14.2 1.0

Manganese binding site 3 out of 4 in the Crystal Structure of Human Arginase-1 Complexed with Inhibitor 1H


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-1 Complexed with Inhibitor 1H within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn502 b:19.0 occ:1.00 OD2 B:ASP234 2.1 14.4 1.0 OD2 B:ASP124 2.1 20.0 1.0 O13 B:1EC501 2.3 18.2 1.0 ND1 B:HIS126 2.3 17.0 1.0 OD2 B:ASP232 2.4 13.6 1.0 OD1 B:ASP234 2.5 12.5 1.0 CG B:ASP234 2.6 15.5 1.0 O23 B:1EC501 2.9 17.2 1.0 CE1 B:HIS126 3.1 16.1 1.0 CG B:ASP124 3.1 20.0 1.0 B10 B:1EC501 3.2 17.8 1.0 CG B:ASP232 3.3 14.9 1.0 CG B:HIS126 3.4 16.7 1.0 MN B:MN503 3.4 20.9 1.0 OD1 B:ASP124 3.4 20.0 1.0 OD1 B:ASP232 3.8 15.5 1.0 CB B:HIS126 3.8 15.8 1.0 O11 B:1EC501 4.0 20.8 1.0 N B:HIS126 4.1 15.6 1.0 CB B:ASP234 4.1 14.1 1.0 OG1 B:THR246 4.1 29.1 1.0 N B:ALA125 4.2 17.7 1.0 CB B:ASP232 4.2 15.2 1.0 NE2 B:HIS126 4.3 16.2 1.0 C8 B:1EC501 4.3 17.6 1.0 C9 B:1EC501 4.4 17.8 1.0 CB B:ASP124 4.4 20.0 1.0 CD2 B:HIS126 4.4 15.7 1.0 OD2 B:ASP128 4.5 15.1 1.0 CA B:HIS126 4.6 15.5 1.0 O B:HOH681 4.6 18.6 1.0 C B:ALA125 4.7 15.5 1.0 CA B:ASP124 4.8 14.2 1.0 CA B:ALA125 4.9 16.1 1.0 C B:ASP124 4.9 15.5 1.0 OD1 B:ASP128 5.0 15.1 1.0

Manganese binding site 4 out of 4 in the Crystal Structure of Human Arginase-1 Complexed with Inhibitor 1H


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-1 Complexed with Inhibitor 1H within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn503 b:20.9 occ:1.00 OD1 B:ASP128 2.2 15.1 1.0 OD1 B:ASP124 2.2 20.0 1.0 ND1 B:HIS101 2.2 16.2 1.0 O11 B:1EC501 2.3 20.8 1.0 OD2 B:ASP232 2.3 13.6 1.0 O13 B:1EC501 2.3 18.2 1.0 B10 B:1EC501 2.8 17.8 1.0 CG B:ASP128 3.1 15.7 1.0 CG B:HIS101 3.1 15.4 1.0 CG B:ASP124 3.2 20.0 1.0 OD2 B:ASP128 3.2 15.1 1.0 CE1 B:HIS101 3.2 14.2 1.0 CG B:ASP232 3.3 14.9 1.0 CB B:HIS101 3.4 17.5 1.0 OD2 B:ASP124 3.4 20.0 1.0 MN B:MN502 3.4 19.0 1.0 O23 B:1EC501 3.6 17.2 1.0 CB B:ASP232 3.6 15.2 1.0 C9 B:1EC501 4.2 17.8 1.0 NE1 B:TRP122 4.3 14.4 1.0 O B:HIS141 4.3 16.6 1.0 CD2 B:HIS101 4.3 15.6 1.0 NE2 B:HIS101 4.4 16.3 1.0 OD1 B:ASP232 4.4 15.5 1.0 CZ2 B:TRP122 4.4 14.6 1.0 CB B:ASP128 4.5 14.7 1.0 CB B:ASP124 4.5 20.0 1.0 CE2 B:TRP122 4.7 14.9 1.0 CG B:GLU277 4.8 16.5 1.0 OE2 B:GLU277 4.9 18.9 1.0 CA B:HIS101 5.0 16.1 1.0 OD2 B:ASP234 5.0 14.4 1.0 CA B:ASP232 5.0 15.3 1.0

A.Golebiowski, R.Paul Beckett, M.Van Zandt, M.K.Ji, D.Whitehouse, T.R.Ryder, E.Jagdmann, M.Andreoli, A.Mazur, M.Padmanilayam, A.Cousido-Siah, A.Mitschler, F.X.Ruiz, A.Podjarny, H.Schroeter. 2-Substituted-2-Amino-6-Boronohexanoic Acids As Arginase Inhibitors. Bioorg.Med.Chem.Lett. V. 23 2027 2013.
ISSN: ISSN 0960-894X
PubMed: 23453840
DOI: 10.1016/J.BMCL.2013.02.024