Manganese in PDB 1o98: 1.4A Crystal Structure of Phosphoglycerate Mutase From Bacillus Stearothermophilus Complexed with 2-Phosphoglycerate

All present enzymatic activity of 1.4A Crystal Structure of Phosphoglycerate Mutase From Bacillus Stearothermophilus Complexed with 2-Phosphoglycerate:
5.4.2.1;

The structure of 1.4A Crystal Structure of Phosphoglycerate Mutase From Bacillus Stearothermophilus Complexed with 2-Phosphoglycerate, PDB code: 1o98 was solved by D.J.Rigden, E.Lamani, J.E.Littlejohn, M.J.Jedrzejas, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.4
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	58.515, 205.787, 125.018, 90.00, 90.00, 90.00
R / Rfree (%)	19 / 19.8

The binding sites of Manganese atom in the 1.4A Crystal Structure of Phosphoglycerate Mutase From Bacillus Stearothermophilus Complexed with 2-Phosphoglycerate (pdb code 1o98). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the 1.4A Crystal Structure of Phosphoglycerate Mutase From Bacillus Stearothermophilus Complexed with 2-Phosphoglycerate, PDB code: 1o98:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the 1.4A Crystal Structure of Phosphoglycerate Mutase From Bacillus Stearothermophilus Complexed with 2-Phosphoglycerate


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of 1.4A Crystal Structure of Phosphoglycerate Mutase From Bacillus Stearothermophilus Complexed with 2-Phosphoglycerate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn601 b:4.5 occ:1.00 OD1 A:ASP403 2.0 8.3 1.0 NE2 A:HIS462 2.1 7.9 1.0 NE2 A:HIS407 2.1 6.1 1.0 O4P A:2PG801 2.1 10.5 1.0 CG A:ASP403 2.7 8.0 1.0 OD2 A:ASP403 2.7 6.4 1.0 O1P A:2PG801 2.8 10.2 1.0 CE1 A:HIS407 3.0 8.0 1.0 P A:2PG801 3.0 10.0 1.0 CE1 A:HIS462 3.0 8.0 1.0 CD2 A:HIS462 3.1 7.6 1.0 CD2 A:HIS407 3.1 5.5 1.0 O A:HOH2461 3.6 11.6 1.0 ND2 A:ASN447 3.8 8.1 1.0 O3P A:2PG801 3.8 9.3 1.0 CE1 A:HIS445 3.9 7.1 1.0 ND1 A:HIS407 4.1 6.6 1.0 O2P A:2PG801 4.1 10.3 1.0 ND1 A:HIS462 4.1 7.8 1.0 C2 A:2PG801 4.1 11.7 1.0 CB A:ASP403 4.2 6.7 1.0 CG A:HIS407 4.2 5.7 1.0 CG A:HIS462 4.2 7.7 1.0 NZ A:LYS336 4.3 8.9 1.0 NE2 A:HIS445 4.3 8.0 1.0 C3 A:2PG801 4.6 12.5 1.0 O A:ASP403 4.7 7.3 1.0 OG A:SER62 4.8 8.7 1.0 O1 A:2PG801 4.8 12.4 1.0 MN A:MN701 4.9 5.7 1.0 OD2 A:ASP12 4.9 7.5 1.0 CA A:ASP403 4.9 7.0 1.0 C A:ASP403 4.9 7.3 1.0 O A:HOH2187 4.9 9.9 1.0 ND1 A:HIS445 4.9 7.5 1.0 CG A:ASN447 4.9 9.0 1.0

Manganese binding site 2 out of 2 in the 1.4A Crystal Structure of Phosphoglycerate Mutase From Bacillus Stearothermophilus Complexed with 2-Phosphoglycerate


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of 1.4A Crystal Structure of Phosphoglycerate Mutase From Bacillus Stearothermophilus Complexed with 2-Phosphoglycerate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn701 b:5.7 occ:1.00 OG A:SER62 2.0 8.7 1.0 OD2 A:ASP444 2.0 9.8 1.0 OD2 A:ASP12 2.1 7.5 1.0 NE2 A:HIS445 2.1 8.0 1.0 CG A:ASP12 2.7 7.4 1.0 OD1 A:ASP12 2.7 8.3 1.0 CG A:ASP444 2.9 9.3 1.0 CD2 A:HIS445 2.9 6.9 1.0 OD1 A:ASP444 3.1 9.7 1.0 CB A:SER62 3.1 8.5 1.0 CE1 A:HIS445 3.2 7.1 1.0 CA A:SER62 3.3 7.5 1.0 N A:SER62 3.5 7.3 1.0 O4P A:2PG801 3.6 10.5 1.0 NZ A:LYS336 3.7 8.9 1.0 CB A:ASP12 4.1 8.4 1.0 CG A:HIS445 4.1 7.3 1.0 ND1 A:HIS445 4.2 7.5 1.0 C A:ASN61 4.3 7.2 1.0 CE A:LYS336 4.3 7.5 1.0 CB A:ASP444 4.3 8.6 1.0 N A:GLY13 4.4 8.5 1.0 OD1 A:ASP403 4.4 8.3 1.0 CG A:ASP403 4.4 8.0 1.0 CE1 A:HIS66 4.5 7.6 1.0 CA A:ASP12 4.5 7.9 1.0 O3P A:2PG801 4.6 9.3 1.0 P A:2PG801 4.6 10.0 1.0 OD2 A:ASP403 4.7 6.4 1.0 O A:ASN61 4.7 9.6 1.0 CD A:LYS336 4.7 7.7 1.0 C A:ASP12 4.8 7.1 1.0 C A:SER62 4.8 8.5 1.0 CB A:ASP403 4.8 6.7 1.0 ND1 A:HIS66 4.8 8.0 1.0 MN A:MN601 4.9 4.5 1.0

D.J.Rigden, L.V.Mello, E.Lamani, J.E.Littlejohn, M.J.Jedrzejas. Insights Into the Catalytic Mechanism of Cofactor-Independent Phosphoglycerate Mutase From X-Ray Crystallography, Simulated Dynamics and Molecular Modeling J.Mol.Biol. V. 328 909 2003.
ISSN: ISSN 0022-2836
PubMed: 12729763
DOI: 10.1016/S0022-2836(03)00350-4