Manganese in PDB 4nwj: Crystal Structure of Phosphopglycerate Mutase From Staphylococcus Aureus in 3-Phosphoglyceric Acid Bound Form.

All present enzymatic activity of Crystal Structure of Phosphopglycerate Mutase From Staphylococcus Aureus in 3-Phosphoglyceric Acid Bound Form.:
5.4.2.12;

The structure of Crystal Structure of Phosphopglycerate Mutase From Staphylococcus Aureus in 3-Phosphoglyceric Acid Bound Form., PDB code: 4nwj was solved by A.Roychowdhury, M.Bose, A.Kundu, A.Gujar, A.K.Das, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.63 / 2.01
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	73.637, 82.841, 89.145, 90.00, 90.00, 90.00
R / Rfree (%)	16.4 / 21.7

The binding sites of Manganese atom in the Crystal Structure of Phosphopglycerate Mutase From Staphylococcus Aureus in 3-Phosphoglyceric Acid Bound Form. (pdb code 4nwj). 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 Phosphopglycerate Mutase From Staphylococcus Aureus in 3-Phosphoglyceric Acid Bound Form., PDB code: 4nwj:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Crystal Structure of Phosphopglycerate Mutase From Staphylococcus Aureus in 3-Phosphoglyceric Acid Bound Form.


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 Phosphopglycerate Mutase From Staphylococcus Aureus in 3-Phosphoglyceric Acid Bound Form. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn601 b:13.8 occ:1.00 OD1 A:ASP397 2.0 11.1 1.0 O A:HOH702 2.0 14.7 1.0 O A:HOH701 2.2 23.9 1.0 NE2 A:HIS401 2.2 20.7 1.0 NE2 A:HIS456 2.2 17.0 1.0 O A:HOH767 2.2 22.1 1.0 CG A:ASP397 2.8 12.9 1.0 OD2 A:ASP397 2.9 12.4 1.0 CE1 A:HIS401 3.1 21.0 1.0 CE1 A:HIS456 3.1 17.8 1.0 CD2 A:HIS401 3.2 18.6 1.0 CD2 A:HIS456 3.2 16.4 1.0 NZ A:LYS330 4.0 13.5 1.0 ND1 A:HIS401 4.3 19.0 1.0 O A:HOH782 4.3 20.7 1.0 ND1 A:HIS456 4.3 16.2 1.0 CB A:ASP397 4.3 12.9 1.0 CG A:HIS401 4.3 17.1 1.0 CG A:HIS456 4.4 16.2 1.0 CE1 A:HIS439 4.4 13.4 1.0 ND2 A:ASN441 4.5 12.1 1.0 OG A:SER62 4.5 13.9 1.0 O A:HOH804 4.6 19.9 1.0 NE2 A:HIS439 4.8 13.0 1.0 SD A:MET398 4.9 15.8 1.0 O A:ASP397 5.0 13.7 1.0

Manganese binding site 2 out of 2 in the Crystal Structure of Phosphopglycerate Mutase From Staphylococcus Aureus in 3-Phosphoglyceric Acid Bound Form.


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 Phosphopglycerate Mutase From Staphylococcus Aureus in 3-Phosphoglyceric Acid Bound Form. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn602 b:8.4 occ:1.00 OG A:SER62 1.8 13.9 1.0 OD1 A:ASP12 1.9 12.7 1.0 OD2 A:ASP438 1.9 13.6 1.0 NE2 A:HIS439 2.0 13.0 1.0 CG A:ASP12 2.6 12.3 1.0 OD2 A:ASP12 2.6 11.6 1.0 CG A:ASP438 2.7 13.2 1.0 OD1 A:ASP438 2.8 11.8 1.0 CD2 A:HIS439 2.9 12.9 1.0 CB A:SER62 3.0 13.3 1.0 CE1 A:HIS439 3.1 13.4 1.0 CA A:SER62 3.3 12.8 1.0 N A:SER62 3.7 13.3 1.0 NZ A:LYS330 3.7 13.5 1.0 CB A:ASP12 4.0 12.7 1.0 CG A:HIS439 4.1 12.7 1.0 ND1 A:HIS439 4.1 12.6 1.0 OD1 A:ASP397 4.2 11.1 1.0 CB A:ASP438 4.2 13.6 1.0 O A:HOH702 4.3 14.7 1.0 CE A:LYS330 4.3 12.4 1.0 CG A:ASP397 4.3 12.9 1.0 N A:GLY13 4.3 11.7 1.0 C A:ASN61 4.3 13.6 1.0 CA A:ASP12 4.5 12.2 1.0 CE1 A:HIS66 4.6 13.5 1.0 C A:SER62 4.6 13.1 1.0 OD2 A:ASP397 4.7 12.4 1.0 CB A:ASP397 4.7 12.9 1.0 O A:ASN61 4.7 12.4 1.0 C A:ASP12 4.8 12.7 1.0 CD A:LYS330 4.8 12.3 1.0 ND1 A:HIS66 4.9 12.8 1.0

A.Roychowdhury, A.Kundu, M.Bose, A.Gujar, S.Mukherjee, A.K.Das. Complete Catalytic Cycle of Cofactor-Independent Phosphoglycerate Mutase Involves A Spring-Loaded Mechanism Febs J. 2015.
ISSN: ISSN 1742-464X
PubMed: 25611430
DOI: 10.1111/FEBS.13205