Manganese in PDB 4hxq: Crystal Structure of Human Arginase-1 Complexed with Inhibitor 14

All present enzymatic activity of Crystal Structure of Human Arginase-1 Complexed with Inhibitor 14:
3.5.3.1;

The structure of Crystal Structure of Human Arginase-1 Complexed with Inhibitor 14, PDB code: 4hxq was solved by A.Cousido-Siah, A.Mitschler, F.X.Ruiz, D.L.Whitehouse, A.Golebiowski, M.Ji, M.Zhang, P.Beckett, R.Sheeler, M.Andreoli, B.Conway, K.Mahboubi, H.Schroeter, M.C.Van Zandt, A.Podjarny, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.11 / 1.45
Space group	P 3
Cell size a, b, c (Å), α, β, γ (°)	90.321, 90.321, 69.534, 90.00, 90.00, 120.00
R / Rfree (%)	18.8 / 20.2

The binding sites of Manganese atom in the Crystal Structure of Human Arginase-1 Complexed with Inhibitor 14 (pdb code 4hxq). 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 14, PDB code: 4hxq:
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 14


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 14 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn902 b:14.8 occ:1.00 OD2 A:ASP234 2.1 8.2 1.0 OD1 A:ASP124 2.1 6.6 1.0 O22 A:X8A901 2.2 10.2 1.0 ND1 A:HIS126 2.3 7.6 1.0 OD1 A:ASP234 2.5 6.6 1.0 OD2 A:ASP232 2.5 8.8 1.0 CG A:ASP234 2.6 6.5 1.0 O20 A:X8A901 2.8 8.4 1.0 CG A:ASP124 3.1 6.4 1.0 B19 A:X8A901 3.1 8.0 1.0 CE1 A:HIS126 3.2 7.5 1.0 MN A:MN903 3.2 11.7 1.0 CG A:ASP232 3.3 6.5 1.0 CG A:HIS126 3.4 7.4 1.0 OD2 A:ASP124 3.4 7.0 1.0 CB A:HIS126 3.7 6.8 1.0 O21 A:X8A901 3.8 10.1 1.0 OD1 A:ASP232 3.8 6.5 1.0 N A:HIS126 4.1 6.4 1.0 CB A:ASP234 4.1 6.2 1.0 OG1 A:THR246 4.1 9.7 1.0 N A:ALA125 4.2 5.7 1.0 CB A:ASP232 4.3 6.4 1.0 C5 A:X8A901 4.3 7.9 1.0 NE2 A:HIS126 4.3 7.3 1.0 CD2 A:HIS126 4.5 7.3 1.0 CB A:ASP124 4.5 6.0 1.0 C4 A:X8A901 4.5 7.8 1.0 OD2 A:ASP128 4.5 7.1 1.0 CA A:HIS126 4.6 6.4 1.0 O A:HOH1006 4.6 7.7 1.0 CB A:ALA125 4.7 6.4 1.0 CA A:ALA125 4.8 5.6 1.0 C A:ALA125 4.8 5.8 1.0 OD1 A:ASP128 4.8 7.6 1.0 CA A:ASP124 4.9 5.2 1.0 C A:ASP124 5.0 5.3 1.0

Manganese binding site 2 out of 4 in the Crystal Structure of Human Arginase-1 Complexed with Inhibitor 14


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 14 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn903 b:11.7 occ:1.00 OD2 A:ASP124 2.0 7.0 1.0 ND1 A:HIS101 2.2 7.3 1.0 OD1 A:ASP128 2.2 7.6 1.0 OD2 A:ASP232 2.2 8.8 1.0 O21 A:X8A901 2.3 10.1 1.0 O22 A:X8A901 2.4 10.2 1.0 CG A:ASP124 3.0 6.4 1.0 B19 A:X8A901 3.1 8.0 1.0 CE1 A:HIS101 3.1 6.4 1.0 CG A:HIS101 3.2 6.2 1.0 CG A:ASP128 3.2 6.6 1.0 MN A:MN902 3.2 14.8 1.0 CG A:ASP232 3.3 6.5 1.0 OD1 A:ASP124 3.3 6.6 1.0 OD2 A:ASP128 3.4 7.1 1.0 CB A:HIS101 3.5 6.8 1.0 CB A:ASP232 3.6 6.4 1.0 O20 A:X8A901 3.8 8.4 1.0 NE2 A:HIS101 4.3 6.4 1.0 CD2 A:HIS101 4.3 6.2 1.0 C5 A:X8A901 4.3 7.9 1.0 NE1 A:TRP122 4.3 5.4 1.0 CB A:ASP124 4.4 6.0 1.0 OD1 A:ASP232 4.4 6.5 1.0 O A:HIS141 4.5 7.2 1.0 CB A:ASP128 4.6 6.2 1.0 CZ2 A:TRP122 4.6 5.3 1.0 CE2 A:TRP122 4.8 5.5 1.0 OD2 A:ASP234 4.8 8.2 1.0 CG A:GLU277 4.9 7.1 1.0 CB A:HIS126 5.0 6.8 1.0 OD1 A:ASP234 5.0 6.6 1.0

Manganese binding site 3 out of 4 in the Crystal Structure of Human Arginase-1 Complexed with Inhibitor 14


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 14 within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn402 b:15.9 occ:1.00 OD2 B:ASP234 2.0 8.6 1.0 O22 B:X8A401 2.1 10.2 1.0 OD1 B:ASP124 2.3 7.3 1.0 ND1 B:HIS126 2.4 7.9 1.0 OD2 B:ASP232 2.4 9.0 1.0 OD1 B:ASP234 2.6 7.3 1.0 O20 B:X8A401 2.6 8.4 1.0 CG B:ASP234 2.6 7.4 1.0 B19 B:X8A401 3.0 8.0 1.0 MN B:MN403 3.2 11.8 1.0 CE1 B:HIS126 3.2 7.7 1.0 CG B:ASP124 3.2 6.9 1.0 CG B:ASP232 3.2 7.1 1.0 OD2 B:ASP124 3.4 7.4 1.0 CG B:HIS126 3.5 7.9 1.0 O21 B:X8A401 3.7 10.1 1.0 OD1 B:ASP232 3.8 7.3 1.0 CB B:HIS126 3.9 7.4 1.0 OG1 B:THR246 4.0 9.7 1.0 CB B:ASP234 4.1 7.7 1.0 C5 B:X8A401 4.2 7.9 1.0 CB B:ASP232 4.2 6.9 1.0 N B:HIS126 4.2 6.8 1.0 NE2 B:HIS126 4.4 7.6 1.0 C4 B:X8A401 4.4 7.8 1.0 N B:ALA125 4.4 6.2 1.0 CD2 B:HIS126 4.5 7.7 1.0 O B:HOH508 4.5 8.7 1.0 OD2 B:ASP128 4.6 7.3 1.0 CB B:ASP124 4.6 7.1 1.0 CA B:HIS126 4.7 6.8 1.0 OD1 B:ASP128 4.8 8.0 1.0 CB B:ALA125 4.9 6.3 1.0 CA B:ASP124 5.0 6.2 1.0

Manganese binding site 4 out of 4 in the Crystal Structure of Human Arginase-1 Complexed with Inhibitor 14


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 14 within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn403 b:11.8 occ:1.00 OD2 B:ASP124 2.1 7.4 1.0 OD1 B:ASP128 2.2 8.0 1.0 ND1 B:HIS101 2.3 8.1 1.0 O21 B:X8A401 2.3 10.1 1.0 OD2 B:ASP232 2.3 9.0 1.0 O22 B:X8A401 2.4 10.2 1.0 B19 B:X8A401 3.0 8.0 1.0 CG B:ASP124 3.0 6.9 1.0 MN B:MN402 3.2 15.9 1.0 CG B:ASP128 3.2 6.9 1.0 CG B:HIS101 3.2 7.6 1.0 CE1 B:HIS101 3.3 7.3 1.0 CG B:ASP232 3.3 7.1 1.0 OD1 B:ASP124 3.3 7.3 1.0 CB B:HIS101 3.4 7.8 1.0 OD2 B:ASP128 3.5 7.3 1.0 CB B:ASP232 3.6 6.9 1.0 O20 B:X8A401 3.8 8.4 1.0 C5 B:X8A401 4.3 7.9 1.0 CD2 B:HIS101 4.3 7.5 1.0 NE2 B:HIS101 4.4 7.4 1.0 NE1 B:TRP122 4.4 6.8 1.0 CB B:ASP124 4.4 7.1 1.0 OD1 B:ASP232 4.4 7.3 1.0 CB B:ASP128 4.5 7.0 1.0 O B:HIS141 4.6 7.2 1.0 CZ2 B:TRP122 4.7 7.3 1.0 CG B:GLU277 4.8 8.0 1.0 OD2 B:ASP234 4.9 8.6 1.0 CE2 B:TRP122 4.9 6.9 1.0 OD1 B:ASP234 4.9 7.3 1.0 CA B:HIS101 4.9 6.9 1.0 CA B:ASP232 5.0 6.5 1.0 OE2 B:GLU277 5.0 8.3 1.0

M.C.Van Zandt, D.L.Whitehouse, A.Golebiowski, M.K.Ji, M.Zhang, R.P.Beckett, G.E.Jagdmann, T.R.Ryder, R.Sheeler, M.Andreoli, B.Conway, K.Mahboubi, G.D'angelo, A.Mitschler, A.Cousido-Siah, F.X.Ruiz, E.I.Howard, A.D.Podjarny, H.Schroeter. Discovery of (R)-2-Amino-6-Borono-2-(2-(Piperidin-1-Yl)Ethyl)Hexanoic Acid and Congeners As Highly Potent Inhibitors of Human Arginases I and II For Treatment of Myocardial Reperfusion Injury. J.Med.Chem. V. 56 2568 2013.
ISSN: ISSN 0022-2623
PubMed: 23472952
DOI: 10.1021/JM400014C