Manganese in PDB 3lp4: Crystal Structure of Human Arginase I in Complex with L-Lysine, 1.90A Resolution.

All present enzymatic activity of Crystal Structure of Human Arginase I in Complex with L-Lysine, 1.90A Resolution.:
3.5.3.1;

The structure of Crystal Structure of Human Arginase I in Complex with L-Lysine, 1.90A Resolution., PDB code: 3lp4 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)	34.20 / 1.90
Space group	P 3
Cell size a, b, c (Å), α, β, γ (°)	90.729, 90.729, 69.509, 90.00, 90.00, 120.00
R / Rfree (%)	15.5 / 20.4

The binding sites of Manganese atom in the Crystal Structure of Human Arginase I in Complex with L-Lysine, 1.90A Resolution. (pdb code 3lp4). 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 L-Lysine, 1.90A Resolution., PDB code: 3lp4:
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 L-Lysine, 1.90A Resolution.


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 L-Lysine, 1.90A Resolution. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn514 b:18.5 occ:1.00 OD1 A:ASP124 1.9 18.0 1.0 ND1 A:HIS126 2.0 14.4 1.0 OD1 A:ASP234 2.2 17.6 1.0 OD2 A:ASP234 2.5 15.7 1.0 OD2 A:ASP232 2.5 17.0 1.0 CE1 A:HIS126 2.6 13.5 1.0 O A:HOH999 2.7 25.6 1.0 CG A:ASP234 2.7 16.5 1.0 CG A:ASP124 2.9 16.8 1.0 CG A:HIS126 3.2 13.9 1.0 OD2 A:ASP124 3.3 14.8 1.0 MN A:MN515 3.3 14.3 1.0 CG A:ASP232 3.4 18.5 1.0 NZ A:LYS401 3.8 24.7 1.0 NE2 A:HIS126 3.8 15.3 1.0 N A:HIS126 3.9 12.7 1.0 N A:ALA125 3.9 14.3 1.0 CB A:HIS126 3.9 14.9 1.0 OD1 A:ASP232 4.0 14.9 1.0 OG1 A:THR246 4.1 16.5 1.0 CD2 A:HIS126 4.2 13.6 1.0 CB A:ASP234 4.2 15.1 1.0 CB A:ASP124 4.3 16.9 1.0 CB A:ASP232 4.3 17.5 1.0 CE A:LYS401 4.4 23.8 1.0 CB A:ALA125 4.4 9.6 1.0 CA A:HIS126 4.5 13.7 1.0 CA A:ALA125 4.6 12.7 1.0 OD1 A:ASP128 4.6 7.8 1.0 C A:ALA125 4.6 11.3 1.0 O A:HOH345 4.7 14.7 1.0 OD2 A:ASP128 4.7 12.8 1.0 CA A:ASP124 4.7 14.6 1.0 C A:ASP124 4.8 12.8 1.0 CD A:LYS401 4.8 24.2 1.0 O A:THR246 4.8 17.3 1.0

Manganese binding site 2 out of 4 in the Crystal Structure of Human Arginase I in Complex with L-Lysine, 1.90A Resolution.


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 L-Lysine, 1.90A Resolution. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn515 b:14.3 occ:1.00 OD2 A:ASP124 1.9 14.8 1.0 O A:HOH999 2.0 25.6 1.0 ND1 A:HIS101 2.2 17.4 1.0 OD2 A:ASP128 2.2 12.8 1.0 OD2 A:ASP232 2.2 17.0 1.0 CG A:ASP124 2.9 16.8 1.0 CE1 A:HIS101 3.1 16.1 1.0 CG A:HIS101 3.2 16.2 1.0 CG A:ASP128 3.2 11.6 1.0 CG A:ASP232 3.2 18.5 1.0 MN A:MN514 3.3 18.5 1.0 OD1 A:ASP124 3.4 18.0 1.0 CB A:HIS101 3.6 17.8 1.0 CB A:ASP232 3.6 17.5 1.0 OD1 A:ASP128 3.6 7.8 1.0 CB A:ASP124 4.2 16.9 1.0 NE2 A:HIS101 4.2 14.7 1.0 NE1 A:TRP122 4.3 15.9 1.0 CD2 A:HIS101 4.3 15.4 1.0 OD1 A:ASP232 4.4 14.9 1.0 NZ A:LYS401 4.4 24.7 1.0 O A:HIS141 4.4 17.8 1.0 CZ2 A:TRP122 4.5 17.7 1.0 CB A:ASP128 4.5 12.1 1.0 OE2 A:GLU277 4.6 17.8 1.0 CG A:GLU277 4.7 17.4 1.0 CE A:LYS401 4.7 23.8 1.0 CE2 A:TRP122 4.7 16.0 1.0 ND1 A:HIS126 4.8 14.4 1.0 OD1 A:ASP234 4.9 17.6 1.0 CA A:ASP232 4.9 16.6 1.0

Manganese binding site 3 out of 4 in the Crystal Structure of Human Arginase I in Complex with L-Lysine, 1.90A Resolution.


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 L-Lysine, 1.90A Resolution. within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn514 b:18.4 occ:1.00 OD1 B:ASP234 2.0 23.1 1.0 OD1 B:ASP124 2.2 19.6 1.0 O B:HOH350 2.2 20.2 1.0 ND1 B:HIS126 2.3 17.5 1.0 OD2 B:ASP232 2.3 16.2 1.0 OD2 B:ASP234 2.5 22.4 1.0 CG B:ASP234 2.6 23.5 1.0 CG B:ASP124 3.0 17.3 1.0 CG B:ASP232 3.0 16.8 1.0 CE1 B:HIS126 3.0 18.0 1.0 OD2 B:ASP124 3.2 17.5 1.0 MN B:MN515 3.2 19.2 1.0 CG B:HIS126 3.4 18.7 1.0 OD1 B:ASP232 3.5 17.0 1.0 NZ B:LYS402 3.7 30.8 1.0 CB B:HIS126 3.9 17.0 1.0 N B:HIS126 4.0 16.2 1.0 OG1 B:THR246 4.0 24.8 1.0 CB B:ASP232 4.0 17.1 1.0 CB B:ASP234 4.1 20.4 1.0 N B:ALA125 4.2 17.5 1.0 CE B:LYS402 4.2 28.7 1.0 NE2 B:HIS126 4.3 19.0 1.0 CB B:ASP124 4.4 17.3 1.0 CD2 B:HIS126 4.4 18.6 1.0 CA B:HIS126 4.5 17.2 1.0 O B:HOH341 4.5 18.9 1.0 OD1 B:ASP128 4.5 15.8 1.0 OD2 B:ASP128 4.6 14.6 1.0 CD B:LYS402 4.6 27.7 1.0 CB B:ALA125 4.7 13.4 1.0 O B:THR246 4.8 26.2 1.0 C B:ALA125 4.8 15.3 1.0 CA B:ALA125 4.9 15.3 1.0 CA B:ASP124 4.9 16.8 1.0 O B:HIS126 4.9 17.5 1.0 CG B:ASP128 5.0 16.6 1.0

Manganese binding site 4 out of 4 in the Crystal Structure of Human Arginase I in Complex with L-Lysine, 1.90A Resolution.


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 L-Lysine, 1.90A Resolution. within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn515 b:19.2 occ:1.00 O B:HOH350 1.8 20.2 1.0 OD2 B:ASP124 2.0 17.5 1.0 OD2 B:ASP128 2.0 14.6 1.0 ND1 B:HIS101 2.2 20.0 1.0 OD2 B:ASP232 2.2 16.2 1.0 CG B:ASP128 3.1 16.6 1.0 CG B:ASP124 3.1 17.3 1.0 CE1 B:HIS101 3.2 19.7 1.0 CG B:HIS101 3.2 20.8 1.0 CG B:ASP232 3.2 16.8 1.0 MN B:MN514 3.2 18.4 1.0 CB B:HIS101 3.5 20.9 1.0 OD1 B:ASP128 3.5 15.8 1.0 OD1 B:ASP124 3.5 19.6 1.0 CB B:ASP232 3.5 17.1 1.0 NZ B:LYS402 4.1 30.8 1.0 NE1 B:TRP122 4.3 13.4 1.0 NE2 B:HIS101 4.3 20.6 1.0 CD2 B:HIS101 4.3 22.7 1.0 CB B:ASP124 4.3 17.3 1.0 CB B:ASP128 4.4 17.1 1.0 OD1 B:ASP232 4.4 17.0 1.0 CZ2 B:TRP122 4.4 15.2 1.0 CE B:LYS402 4.4 28.7 1.0 O B:HIS141 4.6 20.2 1.0 CE2 B:TRP122 4.6 17.2 1.0 CG B:GLU277 4.7 25.6 1.0 O B:HIS126 4.7 17.5 1.0 OD1 B:ASP234 4.8 23.1 1.0 CA B:ASP232 4.9 18.8 1.0 OE2 B:GLU277 4.9 27.9 1.0 ND1 B:HIS126 4.9 17.5 1.0 OD2 B:ASP234 4.9 22.4 1.0 CA B:HIS101 5.0 21.9 1.0

L.Di Costanzo, M.Ilies, K.J.Thorn, D.W.Christianson. Inhibition of Human Arginase I By Substrate and Product Analogues. Arch.Biochem.Biophys. V. 496 101 2010.
ISSN: ISSN 0003-9861
PubMed: 20153713
DOI: 10.1016/J.ABB.2010.02.004