Manganese in PDB 4n7t: Crystal Structure of Phosphorylated Phosphopentomutase From Streptococcus Mutans

All present enzymatic activity of Crystal Structure of Phosphorylated Phosphopentomutase From Streptococcus Mutans:
5.4.2.7;

The structure of Crystal Structure of Phosphorylated Phosphopentomutase From Streptococcus Mutans, PDB code: 4n7t was solved by A.A.Fedorov, E.V.Fedorov, J.Bonanno, S.K.Burley, S.C.Almo, New York Sgxresearch Center For Structural Genomics (Nysgxrc), New Yorkstructural Genomics Research Consortium (Nysgrc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.27 / 2.00
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	69.788, 63.687, 104.765, 90.00, 98.85, 90.00
R / Rfree (%)	17.1 / 20.3

The binding sites of Manganese atom in the Crystal Structure of Phosphorylated Phosphopentomutase From Streptococcus Mutans (pdb code 4n7t). 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 Phosphorylated Phosphopentomutase From Streptococcus Mutans, PDB code: 4n7t:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in the Crystal Structure of Phosphorylated Phosphopentomutase From Streptococcus Mutans


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 Phosphorylated Phosphopentomutase From Streptococcus Mutans within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn501 b:18.9 occ:1.00 OD2 A:ASP13 2.0 17.5 1.0 OD2 A:ASP339 2.1 18.1 1.0 NE2 A:HIS340 2.1 15.4 1.0 OG1 A:TPO92 2.4 38.5 1.0 O2P A:TPO92 2.6 42.8 0.4 CG A:ASP13 2.6 23.3 1.0 OD1 A:ASP13 2.7 18.9 1.0 CG A:ASP339 2.8 19.4 1.0 OD1 A:ASP339 2.9 18.5 1.0 CD2 A:HIS340 2.9 12.1 1.0 P A:TPO92 3.0 35.3 0.7 CE1 A:HIS340 3.1 17.1 1.0 CB A:TPO92 3.5 30.8 1.0 CA A:TPO92 3.9 21.1 1.0 O1P A:TPO92 3.9 40.1 0.5 CG2 A:TPO92 4.0 24.3 1.0 CB A:ASP13 4.0 18.7 1.0 CG A:HIS340 4.1 16.9 1.0 ND1 A:HIS340 4.2 15.5 1.0 CE1 A:HIS351 4.2 17.7 1.0 O3P A:TPO92 4.2 38.3 0.6 CB A:ASP339 4.3 13.1 1.0 N A:SER14 4.3 18.5 1.0 CG A:ASP298 4.4 24.6 1.0 OD2 A:ASP298 4.5 18.0 1.0 CA A:ASP13 4.5 19.0 1.0 NE2 A:HIS351 4.5 19.1 1.0 OD1 A:ASP298 4.6 26.1 1.0 N A:TPO92 4.6 18.5 1.0 CE1 A:HIS96 4.6 16.9 1.0 C A:ASP13 4.6 16.4 1.0 ND1 A:HIS351 4.8 18.2 1.0 CB A:ASP298 4.9 22.0 1.0 MN A:MN502 4.9 21.6 1.0 CA A:SER14 4.9 19.6 1.0

Manganese binding site 2 out of 4 in the Crystal Structure of Phosphorylated Phosphopentomutase From Streptococcus Mutans


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 Phosphorylated Phosphopentomutase From Streptococcus Mutans within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn502 b:21.6 occ:1.00 NE2 A:HIS351 2.0 19.1 1.0 OD1 A:ASP298 2.0 26.1 1.0 NE2 A:HIS303 2.1 24.0 1.0 O A:HOH753 2.2 33.8 1.0 O1P A:TPO92 2.4 40.1 0.5 CG A:ASP298 2.8 24.6 1.0 OD2 A:ASP298 2.9 18.0 1.0 CE1 A:HIS351 3.0 17.7 1.0 CD2 A:HIS351 3.0 17.7 1.0 CD2 A:HIS303 3.0 21.8 1.0 CE1 A:HIS303 3.2 23.1 1.0 O2P A:TPO92 3.4 42.8 0.4 P A:TPO92 3.5 35.3 0.7 OD1 A:ASP165 4.0 61.8 1.0 ND1 A:HIS351 4.1 18.2 1.0 CG A:HIS351 4.1 16.8 1.0 CG A:HIS303 4.2 24.1 1.0 ND1 A:HIS303 4.3 22.2 1.0 CB A:ASP298 4.3 22.0 1.0 ND2 A:ASN342 4.4 16.5 1.0 OG1 A:TPO92 4.5 38.5 1.0 O3P A:TPO92 4.5 38.3 0.6 CE1 A:HIS340 4.6 17.1 1.0 O A:HOH650 4.6 22.4 1.0 NE2 A:HIS340 4.8 15.4 1.0 CB A:ALA164 4.8 50.0 1.0 MN A:MN501 4.9 18.9 1.0

Manganese binding site 3 out of 4 in the Crystal Structure of Phosphorylated Phosphopentomutase From Streptococcus Mutans


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 Phosphorylated Phosphopentomutase From Streptococcus Mutans within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn501 b:15.2 occ:1.00 OD2 B:ASP13 2.0 17.9 1.0 OD2 B:ASP339 2.0 16.1 1.0 NE2 B:HIS340 2.1 12.2 1.0 OG1 B:TPO92 2.5 36.5 1.0 O2P B:TPO92 2.5 43.4 0.5 CG B:ASP13 2.7 24.2 1.0 OD1 B:ASP13 2.7 21.8 1.0 CG B:ASP339 2.8 18.2 1.0 OD1 B:ASP339 3.0 14.8 1.0 CD2 B:HIS340 3.0 12.7 1.0 P B:TPO92 3.1 33.5 0.7 CE1 B:HIS340 3.2 13.9 1.0 CB B:TPO92 3.6 25.9 1.0 CA B:TPO92 3.9 12.2 1.0 CG2 B:TPO92 3.9 21.4 1.0 CB B:ASP13 4.1 16.3 1.0 O1P B:TPO92 4.1 36.6 0.6 CG B:HIS340 4.1 14.0 1.0 O3P B:TPO92 4.1 34.8 0.7 CE1 B:HIS351 4.2 16.1 1.0 ND1 B:HIS340 4.2 14.6 1.0 CB B:ASP339 4.3 11.8 1.0 N B:SER14 4.3 12.7 1.0 CG B:ASP298 4.4 20.7 1.0 NE2 B:HIS351 4.5 16.2 1.0 O B:HOH734 4.5 45.2 1.0 OD1 B:ASP298 4.5 19.2 1.0 CE1 B:HIS96 4.5 12.8 1.0 CA B:ASP13 4.6 12.9 1.0 N B:TPO92 4.6 14.4 1.0 OD2 B:ASP298 4.6 15.6 1.0 C B:ASP13 4.7 14.8 1.0 CB B:ASP298 4.8 16.3 1.0 ND1 B:HIS351 4.8 15.9 1.0 CA B:SER14 4.9 14.3 1.0 MN B:MN502 4.9 22.2 1.0 CB B:SER14 4.9 16.8 1.0

Manganese binding site 4 out of 4 in the Crystal Structure of Phosphorylated Phosphopentomutase From Streptococcus Mutans


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 Phosphorylated Phosphopentomutase From Streptococcus Mutans within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn502 b:22.2 occ:1.00 OD1 B:ASP298 2.0 19.2 1.0 NE2 B:HIS351 2.1 16.2 1.0 NE2 B:HIS303 2.1 20.8 1.0 O1P B:TPO92 2.5 36.6 0.6 O B:HOH757 2.5 41.4 1.0 CG B:ASP298 2.8 20.7 1.0 OD2 B:ASP298 3.0 15.6 1.0 CD2 B:HIS351 3.0 16.2 1.0 CE1 B:HIS303 3.1 24.5 1.0 CE1 B:HIS351 3.1 16.1 1.0 CD2 B:HIS303 3.1 24.7 1.0 O2P B:TPO92 3.2 43.4 0.5 P B:TPO92 3.4 33.5 0.7 ND1 B:HIS351 4.2 15.9 1.0 CG B:HIS351 4.2 17.8 1.0 ND1 B:HIS303 4.2 21.9 1.0 CG B:HIS303 4.2 22.4 1.0 CB B:ASP298 4.3 16.3 1.0 O3P B:TPO92 4.4 34.8 0.7 OD1 B:ASP165 4.4 41.5 1.0 OG1 B:TPO92 4.5 36.5 1.0 ND2 B:ASN342 4.5 21.1 1.0 CE1 B:HIS340 4.7 13.9 1.0 O B:HOH617 4.7 22.5 1.0 NE2 B:HIS340 4.9 12.2 1.0 MN B:MN501 4.9 15.2 1.0

A.A.Fedorov, E.V.Fedorov, J.Bonanno, S.K.Burley, S.C.Almo. Crystal Structure of Phosphorylated Phosphopentomutase From Streptococcus Mutans To Be Published.