Manganese in PDB 1hqx: R308K Arginase Variant

All present enzymatic activity of R308K Arginase Variant:
3.5.3.1;

The structure of R308K Arginase Variant, PDB code: 1hqx was solved by L.T.Lavulo, T.M.Sossong Jr., M.R.Brigham-Burke, M.L.Doyle, J.D.Cox, D.W.Christianson, D.E.Ash, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 3.00
Space group	P 32
Cell size a, b, c (Å), α, β, γ (°)	87.860, 87.860, 112.100, 90.00, 90.00, 120.00
R / Rfree (%)	26.3 / 29.6

The binding sites of Manganese atom in the R308K Arginase Variant (pdb code 1hqx). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 6 binding sites of Manganese where determined in the R308K Arginase Variant, PDB code: 1hqx:
Jump to Manganese binding site number: 1; 2; 3; 4; 5; 6;

Manganese binding site 1 out of 6 in the R308K Arginase Variant


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of R308K Arginase Variant within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn500 b:47.2 occ:1.00 OD2 A:ASP128 1.9 56.4 1.0 OD2 A:ASP232 2.1 45.7 1.0 OD2 A:ASP124 2.3 16.0 1.0 ND1 A:HIS101 2.4 38.6 1.0 CG A:ASP128 2.8 56.3 1.0 MN A:MN501 3.0 50.4 1.0 OD1 A:ASP128 3.2 55.5 1.0 CG A:ASP124 3.2 19.7 1.0 CG A:ASP232 3.2 45.8 1.0 CG A:HIS101 3.2 36.1 1.0 CB A:HIS101 3.3 30.0 1.0 O A:HOH601 3.4 25.2 1.0 OD1 A:ASP124 3.5 17.3 1.0 CE1 A:HIS101 3.5 31.8 1.0 CB A:ASP232 3.8 45.1 1.0 OE2 A:GLU277 3.9 62.0 1.0 CB A:ASP128 4.1 57.5 1.0 OD1 A:ASP232 4.3 45.0 1.0 O A:HIS141 4.3 68.2 1.0 CD2 A:HIS101 4.5 35.9 1.0 OD2 A:ASP234 4.5 48.0 1.0 CB A:ASP124 4.5 15.3 1.0 NE1 A:TRP122 4.6 54.0 1.0 ND1 A:HIS126 4.6 56.1 1.0 NE2 A:HIS101 4.6 34.7 1.0 CZ2 A:TRP122 4.6 54.5 1.0 CG A:GLU277 4.6 59.6 1.0 CD A:GLU277 4.7 60.6 1.0 CA A:HIS101 4.7 52.9 1.0 CE2 A:TRP122 4.9 54.0 1.0

Manganese binding site 2 out of 6 in the R308K Arginase Variant


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of R308K Arginase Variant within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn501 b:50.4 occ:1.00 ND1 A:HIS126 1.9 56.1 1.0 OD1 A:ASP124 2.2 17.3 1.0 OD2 A:ASP234 2.3 48.0 1.0 OD2 A:ASP232 2.4 45.7 1.0 CE1 A:HIS126 2.4 56.6 1.0 O A:HOH601 2.7 25.2 1.0 OD1 A:ASP234 2.7 46.5 1.0 CG A:ASP234 2.9 47.1 1.0 MN A:MN500 3.0 47.2 1.0 CG A:HIS126 3.1 56.5 1.0 CG A:ASP124 3.1 19.7 1.0 CG A:ASP232 3.2 45.8 1.0 OD2 A:ASP124 3.3 16.0 1.0 NE2 A:HIS126 3.5 56.0 1.0 OG1 A:THR246 3.6 43.7 1.0 OD1 A:ASP232 3.7 45.0 1.0 CB A:HIS126 3.8 55.8 1.0 CD2 A:HIS126 3.9 56.0 1.0 OD1 A:ASP128 3.9 55.5 1.0 OD2 A:ASP128 4.0 56.4 1.0 N A:HIS126 4.1 27.8 1.0 CB A:ASP232 4.3 45.1 1.0 CB A:ASP234 4.3 44.9 1.0 CG A:ASP128 4.4 56.3 1.0 CB A:THR246 4.4 41.0 1.0 N A:ALA125 4.5 25.9 1.0 CA A:HIS126 4.5 27.5 1.0 CB A:ASP124 4.6 15.3 1.0 OE2 A:GLU277 4.7 62.0 1.0 CB A:ALA125 5.0 19.0 1.0

Manganese binding site 3 out of 6 in the R308K Arginase Variant


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of R308K Arginase Variant within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn502 b:47.2 occ:1.00 OD2 B:ASP128 1.9 56.4 1.0 OD2 B:ASP232 2.1 45.7 1.0 OD2 B:ASP124 2.3 16.0 1.0 ND1 B:HIS101 2.4 38.6 1.0 CG B:ASP128 2.8 56.3 1.0 MN B:MN503 3.0 50.4 1.0 OD1 B:ASP128 3.2 55.5 1.0 CG B:ASP124 3.2 19.7 1.0 CG B:ASP232 3.2 45.8 1.0 CG B:HIS101 3.2 36.1 1.0 CB B:HIS101 3.3 30.0 1.0 O B:HOH611 3.4 25.2 1.0 OD1 B:ASP124 3.5 17.3 1.0 CE1 B:HIS101 3.5 31.8 1.0 CB B:ASP232 3.8 45.1 1.0 OE2 B:GLU277 3.9 62.0 1.0 CB B:ASP128 4.1 57.5 1.0 OD1 B:ASP232 4.3 45.0 1.0 O B:HIS141 4.3 68.2 1.0 CD2 B:HIS101 4.5 35.9 1.0 OD2 B:ASP234 4.5 48.0 1.0 CB B:ASP124 4.5 15.3 1.0 NE1 B:TRP122 4.6 54.0 1.0 ND1 B:HIS126 4.6 56.1 1.0 NE2 B:HIS101 4.6 34.7 1.0 CZ2 B:TRP122 4.6 54.5 1.0 CG B:GLU277 4.6 59.6 1.0 CD B:GLU277 4.7 60.6 1.0 CA B:HIS101 4.7 52.9 1.0 CE2 B:TRP122 4.9 54.0 1.0

Manganese binding site 4 out of 6 in the R308K Arginase Variant


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of R308K Arginase Variant within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn503 b:50.4 occ:1.00 ND1 B:HIS126 1.9 56.1 1.0 OD1 B:ASP124 2.2 17.3 1.0 OD2 B:ASP234 2.3 48.0 1.0 OD2 B:ASP232 2.4 45.7 1.0 CE1 B:HIS126 2.4 56.6 1.0 O B:HOH611 2.7 25.2 1.0 OD1 B:ASP234 2.7 46.5 1.0 CG B:ASP234 2.9 47.1 1.0 MN B:MN502 3.0 47.2 1.0 CG B:HIS126 3.1 56.5 1.0 CG B:ASP124 3.1 19.7 1.0 CG B:ASP232 3.2 45.8 1.0 OD2 B:ASP124 3.3 16.0 1.0 NE2 B:HIS126 3.5 56.0 1.0 OG1 B:THR246 3.6 43.7 1.0 OD1 B:ASP232 3.7 45.0 1.0 CB B:HIS126 3.8 55.8 1.0 CD2 B:HIS126 3.9 56.0 1.0 OD1 B:ASP128 3.9 55.5 1.0 OD2 B:ASP128 4.0 56.4 1.0 N B:HIS126 4.1 27.8 1.0 CB B:ASP232 4.3 45.1 1.0 CB B:ASP234 4.3 44.9 1.0 CG B:ASP128 4.4 56.3 1.0 CB B:THR246 4.4 41.0 1.0 N B:ALA125 4.5 25.9 1.0 CA B:HIS126 4.5 27.5 1.0 CB B:ASP124 4.6 15.3 1.0 OE2 B:GLU277 4.7 62.0 1.0 CB B:ALA125 5.0 19.0 1.0

Manganese binding site 5 out of 6 in the R308K Arginase Variant


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 5 of R308K Arginase Variant within 5.0Å range: probe atom residue distance (Å) B Occ C:Mn504 b:47.2 occ:1.00 OD2 C:ASP128 1.9 56.4 1.0 OD2 C:ASP232 2.1 45.7 1.0 OD2 C:ASP124 2.3 16.0 1.0 ND1 C:HIS101 2.4 38.6 1.0 CG C:ASP128 2.8 56.3 1.0 MN C:MN505 3.0 50.4 1.0 OD1 C:ASP128 3.2 55.5 1.0 CG C:ASP124 3.2 19.7 1.0 CG C:ASP232 3.2 45.8 1.0 CG C:HIS101 3.2 36.1 1.0 CB C:HIS101 3.3 30.0 1.0 O C:HOH620 3.4 25.2 1.0 OD1 C:ASP124 3.5 17.3 1.0 CE1 C:HIS101 3.5 31.8 1.0 CB C:ASP232 3.8 45.1 1.0 OE2 C:GLU277 3.9 62.0 1.0 CB C:ASP128 4.1 57.5 1.0 OD1 C:ASP232 4.3 45.0 1.0 O C:HIS141 4.3 68.2 1.0 CD2 C:HIS101 4.5 35.9 1.0 OD2 C:ASP234 4.5 48.0 1.0 CB C:ASP124 4.5 15.3 1.0 NE1 C:TRP122 4.6 54.0 1.0 ND1 C:HIS126 4.6 56.1 1.0 NE2 C:HIS101 4.6 34.7 1.0 CZ2 C:TRP122 4.6 54.5 1.0 CG C:GLU277 4.6 59.6 1.0 CD C:GLU277 4.7 60.6 1.0 CA C:HIS101 4.7 52.9 1.0 CE2 C:TRP122 4.9 54.0 1.0

Manganese binding site 6 out of 6 in the R308K Arginase Variant


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 6 of R308K Arginase Variant within 5.0Å range: probe atom residue distance (Å) B Occ C:Mn505 b:50.4 occ:1.00 ND1 C:HIS126 1.9 56.1 1.0 OD1 C:ASP124 2.2 17.3 1.0 OD2 C:ASP234 2.3 48.0 1.0 OD2 C:ASP232 2.4 45.7 1.0 CE1 C:HIS126 2.4 56.6 1.0 O C:HOH620 2.7 25.2 1.0 OD1 C:ASP234 2.7 46.5 1.0 CG C:ASP234 2.9 47.1 1.0 MN C:MN504 3.0 47.2 1.0 CG C:HIS126 3.1 56.5 1.0 CG C:ASP124 3.1 19.7 1.0 CG C:ASP232 3.2 45.8 1.0 OD2 C:ASP124 3.3 16.0 1.0 NE2 C:HIS126 3.5 56.0 1.0 OG1 C:THR246 3.6 43.7 1.0 OD1 C:ASP232 3.7 45.0 1.0 CB C:HIS126 3.8 55.8 1.0 CD2 C:HIS126 3.9 56.0 1.0 OD1 C:ASP128 3.9 55.5 1.0 OD2 C:ASP128 4.0 56.4 1.0 N C:HIS126 4.1 27.8 1.0 CB C:ASP232 4.3 45.1 1.0 CB C:ASP234 4.3 44.9 1.0 CG C:ASP128 4.4 56.3 1.0 CB C:THR246 4.4 41.0 1.0 N C:ALA125 4.5 25.9 1.0 CA C:HIS126 4.5 27.5 1.0 CB C:ASP124 4.5 15.3 1.0 OE2 C:GLU277 4.7 62.0 1.0 CB C:ALA125 5.0 19.0 1.0

L.T.Lavulo, T.M.Sossong Jr., M.R.Brigham-Burke, M.L.Doyle, J.D.Cox, D.W.Christianson, D.E.Ash. Subunit-Subunit Interactions in Trimeric Arginase. Generation of Active Monomers By Mutation of A Single Amino Acid. J.Biol.Chem. V. 276 14242 2001.
ISSN: ISSN 0021-9258
PubMed: 11278703
DOI: 10.1074/JBC.M010575200