Manganese in PDB 4qsf: Crystal Structure of Amidohydrolase PMI1525 (Target Efi-500319) From Proteus Mirabilis HI4320, A Complex with Butyric Acid and Manganese

The structure of Crystal Structure of Amidohydrolase PMI1525 (Target Efi-500319) From Proteus Mirabilis HI4320, A Complex with Butyric Acid and Manganese, PDB code: 4qsf was solved by Y.Patskovsky, R.Toro, D.F.Xiang, F.M.Raushel, J.A.Gerlt, S.C.Almo, Enzymefunction Initiative (Efi), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.46 / 1.65
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	101.269, 101.269, 65.493, 90.00, 90.00, 120.00
R / Rfree (%)	15.5 / 18.1

The binding sites of Manganese atom in the Crystal Structure of Amidohydrolase PMI1525 (Target Efi-500319) From Proteus Mirabilis HI4320, A Complex with Butyric Acid and Manganese (pdb code 4qsf). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Crystal Structure of Amidohydrolase PMI1525 (Target Efi-500319) From Proteus Mirabilis HI4320, A Complex with Butyric Acid and Manganese, PDB code: 4qsf:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Crystal Structure of Amidohydrolase PMI1525 (Target Efi-500319) From Proteus Mirabilis HI4320, A Complex with Butyric Acid and Manganese


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 Amidohydrolase PMI1525 (Target Efi-500319) From Proteus Mirabilis HI4320, A Complex with Butyric Acid and Manganese within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn401 b:21.0 occ:0.80 O1 A:BUA403 2.1 29.3 1.0 NE2 A:HIS25 2.1 22.5 1.0 NE2 A:HIS23 2.1 20.2 1.0 OE2 A:GLU166 2.2 25.7 1.0 OD1 A:ASP294 2.2 22.5 1.0 C4 A:BUA403 3.0 67.4 1.0 CD2 A:HIS23 3.0 20.7 1.0 CD2 A:HIS25 3.1 18.0 1.0 CG A:ASP294 3.1 19.1 1.0 CE1 A:HIS23 3.1 23.0 1.0 CE1 A:HIS25 3.1 22.6 1.0 CD A:GLU166 3.2 23.5 1.0 C3 A:BUA403 3.5 37.3 1.0 OE1 A:GLU166 3.5 23.7 1.0 OD2 A:ASP294 3.5 22.4 1.0 MN A:MN402 3.7 25.5 0.8 O2 A:BUA403 4.0 37.1 1.0 CG A:HIS23 4.2 17.1 1.0 ND1 A:HIS23 4.2 21.3 1.0 ND1 A:HIS25 4.2 19.7 1.0 CG A:HIS25 4.3 17.6 1.0 CE1 A:HIS229 4.3 35.7 1.0 C2 A:BUA403 4.4 70.1 1.0 CB A:ASP294 4.4 16.9 1.0 NE2 A:HIS229 4.5 25.8 1.0 CG A:GLU166 4.5 20.8 1.0 CB A:ALA95 4.6 19.1 1.0 C1 A:BUA403 4.9 40.9 1.0 CA A:ASP294 4.9 18.0 1.0

Manganese binding site 2 out of 2 in the Crystal Structure of Amidohydrolase PMI1525 (Target Efi-500319) From Proteus Mirabilis HI4320, A Complex with Butyric Acid and Manganese


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 Amidohydrolase PMI1525 (Target Efi-500319) From Proteus Mirabilis HI4320, A Complex with Butyric Acid and Manganese within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn402 b:25.5 occ:0.80 ND1 A:HIS199 2.1 20.6 1.0 OE1 A:GLU166 2.1 23.7 1.0 O2 A:BUA403 2.1 37.1 1.0 NE2 A:HIS229 2.2 25.8 1.0 O1 A:BUA403 2.2 29.3 1.0 C4 A:BUA403 2.6 67.4 1.0 CE1 A:HIS199 3.0 23.2 1.0 CD A:GLU166 3.0 23.5 1.0 CE1 A:HIS229 3.1 35.7 1.0 CD2 A:HIS229 3.1 29.9 1.0 CG A:HIS199 3.1 16.3 1.0 OE2 A:GLU166 3.4 25.7 1.0 CB A:HIS199 3.6 16.1 1.0 MN A:MN401 3.7 21.0 0.8 OH A:TYR126 4.0 29.2 1.0 C3 A:BUA403 4.0 37.3 1.0 NE2 A:HIS199 4.1 23.9 1.0 CE1 A:TYR126 4.1 23.4 1.0 CD2 A:HIS199 4.2 21.6 1.0 ND1 A:HIS229 4.2 27.8 1.0 CA A:HIS199 4.3 13.6 1.0 CG A:HIS229 4.3 22.7 1.0 CG A:GLU166 4.3 20.8 1.0 NE2 A:HIS23 4.3 20.2 1.0 CE1 A:HIS23 4.5 23.0 1.0 CZ A:TYR126 4.5 24.6 1.0 OD2 A:ASP294 4.9 22.4 1.0 C2 A:BUA403 4.9 70.1 1.0 CB A:GLU166 4.9 21.6 1.0

Y.Patskovsky, R.Toro, D.F.Xiang, F.M.Raushel, S.C.Almo. Crystal Structure of Amidohydrolase PMI1525 From Proteus Mirabilis HI4320 To Be Published.