Manganese in PDB 1tbl: H141N Mutant of Rat Liver Arginase I

All present enzymatic activity of H141N Mutant of Rat Liver Arginase I:
3.5.3.1;

The structure of H141N Mutant of Rat Liver Arginase I, PDB code: 1tbl was solved by E.Cama, J.D.Cox, D.E.Ash, D.W.Christianson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.56 / 3.10
Space group	P 32
Cell size a, b, c (Å), α, β, γ (°)	88.332, 88.332, 113.417, 90.00, 90.00, 120.00
R / Rfree (%)	29.8 / 30.6

The binding sites of Manganese atom in the H141N Mutant of Rat Liver Arginase I (pdb code 1tbl). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 6 binding sites of Manganese where determined in the H141N Mutant of Rat Liver Arginase I, PDB code: 1tbl:
Jump to Manganese binding site number: 1; 2; 3; 4; 5; 6;

Manganese binding site 1 out of 6 in the H141N Mutant of Rat Liver Arginase I


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of H141N Mutant of Rat Liver Arginase I within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn1 b:40.3 occ:1.00 OD2 A:ASP234 2.1 58.5 1.0 ND1 A:HIS126 2.4 59.7 1.0 OD1 A:ASP234 2.4 58.4 1.0 OD2 A:ASP232 2.5 38.8 1.0 OD1 A:ASP124 2.5 63.3 1.0 CG A:ASP234 2.5 56.9 1.0 O A:HOH800 2.6 91.5 1.0 CE1 A:HIS126 3.0 57.2 1.0 CG A:ASP124 3.2 65.3 1.0 OD2 A:ASP124 3.3 67.5 1.0 CG A:ASP232 3.3 40.3 1.0 CG A:HIS126 3.3 60.5 1.0 MN A:MN2 3.3 59.4 1.0 OD1 A:ASP232 3.7 38.6 1.0 CB A:HIS126 3.8 63.5 1.0 OD1 A:ASP128 3.9 72.0 1.0 NE2 A:HIS126 3.9 56.4 1.0 CB A:ASP234 4.0 53.0 1.0 OD2 A:ASP128 4.1 71.9 1.0 CD2 A:HIS126 4.1 57.6 1.0 CB A:ASP232 4.3 43.5 1.0 CG A:ASP128 4.4 73.2 1.0 N A:HIS126 4.5 69.8 1.0 CB A:ASP124 4.7 64.7 1.0 N A:ALA125 4.7 64.0 1.0 CA A:HIS126 4.7 70.9 1.0 OG1 A:THR246 4.9 57.4 1.0

Manganese binding site 2 out of 6 in the H141N Mutant of Rat Liver Arginase I


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of H141N Mutant of Rat Liver Arginase I within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn2 b:59.4 occ:1.00 ND1 A:HIS101 2.0 60.3 1.0 OD2 A:ASP128 2.2 71.9 1.0 OD2 A:ASP124 2.4 67.5 1.0 O A:HOH800 2.4 91.5 1.0 OD2 A:ASP232 2.5 38.8 1.0 CG A:HIS101 2.9 61.2 1.0 CG A:ASP128 2.9 73.2 1.0 CB A:HIS101 3.1 62.5 1.0 CE1 A:HIS101 3.1 58.9 1.0 OD1 A:ASP128 3.3 72.0 1.0 MN A:MN1 3.3 40.3 1.0 CG A:ASP124 3.5 65.3 1.0 CG A:ASP232 3.6 40.3 1.0 OD1 A:ASP124 4.0 63.3 1.0 CB A:ASP128 4.1 74.4 1.0 CD2 A:HIS101 4.1 60.4 1.0 CB A:ASP232 4.1 43.5 1.0 NE2 A:HIS101 4.1 60.5 1.0 O A:ASN141 4.2 89.4 1.0 OD2 A:ASP234 4.4 58.5 1.0 NE1 A:TRP122 4.5 64.6 1.0 CZ2 A:TRP122 4.6 63.3 1.0 CA A:HIS101 4.6 68.5 1.0 OD1 A:ASP232 4.7 38.6 1.0 CB A:ASP124 4.8 64.7 1.0 CE2 A:TRP122 4.9 63.5 1.0 OE2 A:GLU277 5.0 72.0 1.0 CG A:GLU277 5.0 73.0 1.0

Manganese binding site 3 out of 6 in the H141N Mutant of Rat Liver Arginase I


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of H141N Mutant of Rat Liver Arginase I within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn3 b:37.0 occ:1.00 OD2 B:ASP234 2.1 58.5 1.0 ND1 B:HIS126 2.4 59.7 1.0 OD1 B:ASP234 2.5 58.4 1.0 OD2 B:ASP232 2.5 38.8 1.0 OD1 B:ASP124 2.5 63.3 1.0 CG B:ASP234 2.6 56.9 1.0 O B:HOH801 2.6 56.1 1.0 CE1 B:HIS126 3.0 57.2 1.0 CG B:ASP124 3.3 65.3 1.0 CG B:HIS126 3.3 60.5 1.0 OD2 B:ASP124 3.3 67.5 1.0 CG B:ASP232 3.3 40.3 1.0 MN B:MN4 3.3 56.8 1.0 OD1 B:ASP232 3.7 38.6 1.0 CB B:HIS126 3.8 63.5 1.0 OD1 B:ASP128 3.9 72.0 1.0 NE2 B:HIS126 3.9 56.4 1.0 CB B:ASP234 4.0 53.0 1.0 CD2 B:HIS126 4.1 57.6 1.0 OD2 B:ASP128 4.1 71.9 1.0 CB B:ASP232 4.4 43.5 1.0 CG B:ASP128 4.4 73.2 1.0 N B:HIS126 4.5 69.8 1.0 CB B:ASP124 4.7 64.7 1.0 CA B:HIS126 4.8 70.9 1.0 N B:ALA125 4.8 64.0 1.0 OG1 B:THR246 4.9 57.4 1.0

Manganese binding site 4 out of 6 in the H141N Mutant of Rat Liver Arginase I


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of H141N Mutant of Rat Liver Arginase I within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn4 b:56.8 occ:1.00 ND1 B:HIS101 2.1 60.3 1.0 OD2 B:ASP128 2.1 71.9 1.0 O B:HOH801 2.3 56.1 1.0 OD2 B:ASP124 2.5 67.5 1.0 OD2 B:ASP232 2.5 38.8 1.0 CG B:ASP128 2.9 73.2 1.0 CG B:HIS101 2.9 61.2 1.0 CB B:HIS101 3.1 62.5 1.0 CE1 B:HIS101 3.1 58.9 1.0 OD1 B:ASP128 3.3 72.0 1.0 MN B:MN3 3.3 37.0 1.0 CG B:ASP124 3.6 65.3 1.0 CG B:ASP232 3.6 40.3 1.0 OD1 B:ASP124 4.0 63.3 1.0 CB B:ASP128 4.0 74.4 1.0 CD2 B:HIS101 4.1 60.4 1.0 CB B:ASP232 4.2 43.5 1.0 NE2 B:HIS101 4.2 60.5 1.0 O B:ASN141 4.2 89.4 1.0 OD2 B:ASP234 4.4 58.5 1.0 NE1 B:TRP122 4.6 64.6 1.0 CZ2 B:TRP122 4.6 63.3 1.0 CA B:HIS101 4.6 68.5 1.0 OD1 B:ASP232 4.7 38.6 1.0 CB B:ASP124 4.8 64.7 1.0 OE2 B:GLU277 5.0 72.0 1.0 CE2 B:TRP122 5.0 63.5 1.0 CG B:GLU277 5.0 73.0 1.0

Manganese binding site 5 out of 6 in the H141N Mutant of Rat Liver Arginase I


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 5 of H141N Mutant of Rat Liver Arginase I within 5.0Å range: probe atom residue distance (Å) B Occ C:Mn5 b:28.4 occ:1.00 OD2 C:ASP234 2.1 58.5 1.0 ND1 C:HIS126 2.4 59.7 1.0 OD1 C:ASP234 2.4 58.4 1.0 OD2 C:ASP232 2.5 38.8 1.0 CG C:ASP234 2.5 56.9 1.0 OD1 C:ASP124 2.5 63.3 1.0 O C:HOH802 2.7 32.3 1.0 CE1 C:HIS126 3.0 57.2 1.0 CG C:HIS126 3.3 60.5 1.0 CG C:ASP124 3.3 65.3 1.0 CG C:ASP232 3.3 40.3 1.0 O C:HOH818 3.3 21.9 1.0 OD2 C:ASP124 3.3 67.5 1.0 MN C:MN320 3.3 56.5 1.0 OD1 C:ASP232 3.7 38.6 1.0 CB C:HIS126 3.9 63.5 1.0 NE2 C:HIS126 3.9 56.4 1.0 OD1 C:ASP128 3.9 72.0 1.0 CB C:ASP234 4.0 53.0 1.0 CD2 C:HIS126 4.1 57.6 1.0 OD2 C:ASP128 4.1 71.9 1.0 CB C:ASP232 4.4 43.5 1.0 CG C:ASP128 4.5 73.2 1.0 N C:HIS126 4.5 69.8 1.0 CB C:ASP124 4.7 64.7 1.0 N C:ALA125 4.8 64.0 1.0 CA C:HIS126 4.8 70.9 1.0 OG1 C:THR246 4.9 57.4 1.0

Manganese binding site 6 out of 6 in the H141N Mutant of Rat Liver Arginase I


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 6 of H141N Mutant of Rat Liver Arginase I within 5.0Å range: probe atom residue distance (Å) B Occ C:Mn320 b:56.5 occ:1.00 ND1 C:HIS101 2.0 60.3 1.0 OD2 C:ASP128 2.2 71.9 1.0 OD2 C:ASP124 2.4 67.5 1.0 OD2 C:ASP232 2.4 38.8 1.0 O C:HOH802 2.5 32.3 1.0 CG C:HIS101 2.9 61.2 1.0 CG C:ASP128 2.9 73.2 1.0 CB C:HIS101 3.1 62.5 1.0 CE1 C:HIS101 3.1 58.9 1.0 OD1 C:ASP128 3.3 72.0 1.0 MN C:MN5 3.3 28.4 1.0 CG C:ASP124 3.5 65.3 1.0 CG C:ASP232 3.6 40.3 1.0 OD1 C:ASP124 4.0 63.3 1.0 CD2 C:HIS101 4.1 60.4 1.0 CB C:ASP128 4.1 74.4 1.0 CB C:ASP232 4.1 43.5 1.0 NE2 C:HIS101 4.2 60.5 1.0 O C:ASN141 4.3 89.4 1.0 OD2 C:ASP234 4.4 58.5 1.0 NE1 C:TRP122 4.6 64.6 1.0 CA C:HIS101 4.6 68.5 1.0 OD1 C:ASP232 4.6 38.6 1.0 CZ2 C:TRP122 4.6 63.3 1.0 CB C:ASP124 4.8 64.7 1.0 CG C:GLU277 4.9 73.0 1.0 OE2 C:GLU277 4.9 72.0 1.0 CE2 C:TRP122 5.0 63.5 1.0

D.M.Colleluori, R.S.Reczkowski, F.A.Emig, E.Cama, J.D.Cox, L.R.Scolnick, K.Compher, K.Jude, S.Han, R.E.Viola, D.W.Christianson, D.E.Ash. Probing the Role of the Hyper-Reactive Histidine Residue of Arginase. Arch.Biochem.Biophys. V. 444 15 2005.
ISSN: ISSN 0003-9861
PubMed: 16266687
DOI: 10.1016/J.ABB.2005.09.009