Manganese in PDB 1wva: Crystal Structure of Human Arginase I From Twinned Crystal

All present enzymatic activity of Crystal Structure of Human Arginase I From Twinned Crystal:
3.5.3.1;

The structure of Crystal Structure of Human Arginase I From Twinned Crystal, PDB code: 1wva was solved by L.Di Costanzo, G.Sabio, A.Mora, P.C.Rodriguez, A.C.Ochoa, F.Centeno, D.W.Christianson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.94
Space group	P 3
Cell size a, b, c (Å), α, β, γ (°)	90.602, 90.602, 69.311, 90.00, 90.00, 120.00
R / Rfree (%)	15 / 20.9

The binding sites of Manganese atom in the Crystal Structure of Human Arginase I From Twinned Crystal (pdb code 1wva). 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 From Twinned Crystal, PDB code: 1wva:
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 From Twinned Crystal


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 From Twinned Crystal within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn2314 b:18.2 occ:1.00 OD2 A:ASP128 2.2 12.4 1.0 OD2 A:ASP124 2.2 14.4 1.0 ND1 A:HIS101 2.3 14.0 1.0 OD2 A:ASP232 2.3 21.2 1.0 O1 A:S2C1317 2.4 21.7 1.0 O2 A:S2C1317 2.6 19.6 1.0 B A:S2C1317 3.0 19.4 1.0 CG A:HIS101 3.2 15.1 1.0 CG A:ASP128 3.2 9.6 1.0 CG A:ASP124 3.2 12.0 1.0 CG A:ASP232 3.3 17.8 1.0 CB A:HIS101 3.3 16.9 1.0 CE1 A:HIS101 3.3 14.0 1.0 MN A:MN2315 3.4 14.1 1.0 OD1 A:ASP124 3.5 13.6 1.0 OD1 A:ASP128 3.5 2.1 1.0 CB A:ASP232 3.6 16.8 1.0 O3 A:S2C1317 3.7 17.9 1.0 O A:HIS141 4.3 16.2 1.0 CE A:S2C1317 4.4 21.3 1.0 CD2 A:HIS101 4.4 14.8 1.0 NE1 A:TRP122 4.4 16.6 1.0 NE2 A:HIS101 4.4 12.9 1.0 OD1 A:ASP232 4.5 13.5 1.0 CG A:GLU277 4.5 16.4 1.0 CB A:ASP128 4.5 12.4 1.0 CZ2 A:TRP122 4.5 16.4 1.0 CB A:ASP124 4.6 14.0 1.0 CE2 A:TRP122 4.8 16.2 1.0 OD2 A:ASP234 4.8 11.5 1.0 CA A:HIS101 4.9 18.0 1.0 OE2 A:GLU277 4.9 18.0 1.0 CA A:ASP232 4.9 16.5 1.0

Manganese binding site 2 out of 4 in the Crystal Structure of Human Arginase I From Twinned Crystal


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 From Twinned Crystal within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn2315 b:14.1 occ:1.00 OD2 A:ASP234 2.1 11.5 1.0 O1 A:S2C1317 2.2 21.7 1.0 OD1 A:ASP124 2.2 13.6 1.0 ND1 A:HIS126 2.3 5.7 1.0 OD1 A:ASP234 2.4 10.5 1.0 OD2 A:ASP232 2.5 21.2 1.0 CG A:ASP234 2.6 15.4 1.0 O3 A:S2C1317 2.9 17.9 1.0 B A:S2C1317 3.1 19.4 1.0 CE1 A:HIS126 3.2 9.3 1.0 CG A:ASP232 3.2 17.8 1.0 CG A:ASP124 3.2 12.0 1.0 MN A:MN2314 3.4 18.2 1.0 CG A:HIS126 3.4 8.8 1.0 OD2 A:ASP124 3.5 14.4 1.0 OD1 A:ASP232 3.6 13.5 1.0 CB A:HIS126 3.8 10.3 1.0 N A:HIS126 4.0 11.5 1.0 O2 A:S2C1317 4.1 19.6 1.0 CB A:ASP234 4.1 13.6 1.0 CB A:ASP232 4.1 16.8 1.0 N A:ALA125 4.1 13.8 1.0 CD A:S2C1317 4.2 23.3 1.0 CE A:S2C1317 4.2 21.3 1.0 NE2 A:HIS126 4.3 7.0 1.0 CD2 A:HIS126 4.5 9.6 1.0 CB A:ASP124 4.5 14.0 1.0 OD1 A:ASP128 4.6 2.1 1.0 CA A:HIS126 4.6 10.4 1.0 CB A:ALA125 4.6 11.9 1.0 OD2 A:ASP128 4.7 12.4 1.0 O A:HOH2347 4.7 13.0 1.0 CA A:ALA125 4.8 12.2 1.0 C A:ALA125 4.8 11.2 1.0 CA A:ASP124 4.9 13.0 1.0 O A:HOH2354 5.0 16.2 1.0 C A:ASP124 5.0 14.5 1.0 CA A:ASP234 5.0 12.1 1.0

Manganese binding site 3 out of 4 in the Crystal Structure of Human Arginase I From Twinned Crystal


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 From Twinned Crystal within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn1314 b:15.1 occ:1.00 OD2 B:ASP124 2.1 10.6 1.0 OD2 B:ASP128 2.2 12.2 1.0 O1 B:S2C1316 2.3 19.0 1.0 ND1 B:HIS101 2.3 15.2 1.0 OD2 B:ASP232 2.4 17.0 1.0 O2 B:S2C1316 2.6 16.2 1.0 B B:S2C1316 3.0 18.4 1.0 CG B:ASP124 3.1 13.5 1.0 CG B:ASP128 3.2 10.9 1.0 CG B:HIS101 3.3 15.3 1.0 CE1 B:HIS101 3.3 14.2 1.0 CG B:ASP232 3.3 16.0 1.0 OD1 B:ASP124 3.5 12.8 1.0 MN B:MN1315 3.5 15.6 1.0 OD1 B:ASP128 3.5 10.4 1.0 CB B:HIS101 3.5 15.7 1.0 O3 B:S2C1316 3.6 16.4 1.0 CB B:ASP232 3.7 14.7 1.0 CE B:S2C1316 4.3 20.4 1.0 O B:HIS141 4.3 10.9 1.0 OD1 B:ASP232 4.4 13.3 1.0 NE2 B:HIS101 4.4 13.2 1.0 CB B:ASP124 4.4 14.0 1.0 CD2 B:HIS101 4.4 14.1 1.0 NE1 B:TRP122 4.4 13.2 1.0 CZ2 B:TRP122 4.5 11.6 1.0 CB B:ASP128 4.5 11.9 1.0 CE2 B:TRP122 4.8 11.7 1.0 CG B:GLU277 4.8 18.6 1.0 OE2 B:GLU277 5.0 20.5 1.0

Manganese binding site 4 out of 4 in the Crystal Structure of Human Arginase I From Twinned Crystal


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 From Twinned Crystal within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn1315 b:15.6 occ:1.00 OD1 B:ASP234 2.2 16.7 1.0 OD1 B:ASP124 2.2 12.8 1.0 ND1 B:HIS126 2.3 6.1 1.0 O1 B:S2C1316 2.4 19.0 1.0 OD2 B:ASP232 2.4 17.0 1.0 OD2 B:ASP234 2.5 8.8 1.0 CG B:ASP234 2.7 14.5 1.0 O3 B:S2C1316 2.8 16.4 1.0 CE1 B:HIS126 3.1 4.4 1.0 B B:S2C1316 3.1 18.4 1.0 CG B:ASP124 3.2 13.5 1.0 CG B:HIS126 3.4 6.3 1.0 CG B:ASP232 3.4 16.0 1.0 MN B:MN1314 3.5 15.1 1.0 OD2 B:ASP124 3.5 10.6 1.0 CB B:HIS126 3.8 9.5 1.0 N B:HIS126 4.0 8.8 1.0 OD1 B:ASP232 4.1 13.3 1.0 O2 B:S2C1316 4.1 16.2 1.0 N B:ALA125 4.1 8.7 1.0 CD B:S2C1316 4.1 23.4 1.0 CE B:S2C1316 4.2 20.4 1.0 CB B:ASP234 4.2 12.6 1.0 NE2 B:HIS126 4.3 4.5 1.0 CB B:ASP232 4.4 14.7 1.0 CD2 B:HIS126 4.4 5.9 1.0 CA B:HIS126 4.5 8.9 1.0 CB B:ASP124 4.6 14.0 1.0 O B:HOH1319 4.6 15.2 1.0 CB B:ALA125 4.7 7.6 1.0 OD1 B:ASP128 4.7 10.4 1.0 C B:ALA125 4.7 7.2 1.0 CA B:ALA125 4.8 8.4 1.0 O B:THR246 4.8 13.6 1.0 CA B:ASP124 4.9 12.5 1.0 OD2 B:ASP128 5.0 12.2 1.0 C B:ASP124 5.0 10.9 1.0

L.Di Costanzo, G.Sabio, A.Mora, P.C.Rodriguez, A.C.Ochoa, F.Centeno, D.W.Christianson. Crystal Structure of Human Arginase I at 1.29 A Resolution and Exploration of Inhibition in the Immune Response Proc.Natl.Acad.Sci.Usa V. 102 13058 2005.
ISSN: ISSN 0027-8424
PubMed: 16141327
DOI: 10.1073/PNAS.0504027102