Manganese in PDB 4ptj: Ensemble Model For Escherichia Coli Dihydrofolate Reductase at 277K

All present enzymatic activity of Ensemble Model For Escherichia Coli Dihydrofolate Reductase at 277K:
1.5.1.3;

The structure of Ensemble Model For Escherichia Coli Dihydrofolate Reductase at 277K, PDB code: 4ptj was solved by D.A.Keedy, H.Van Den Bedem, D.A.Sivak, G.A.Petsko, D.Ringe, M.A.Wilson, J.S.Fraser, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.40 / 1.05
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	34.299, 45.521, 98.711, 90.00, 90.00, 90.00
R / Rfree (%)	13.6 / 16.6

The binding sites of Manganese atom in the Ensemble Model For Escherichia Coli Dihydrofolate Reductase at 277K (pdb code 4ptj). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Ensemble Model For Escherichia Coli Dihydrofolate Reductase at 277K, PDB code: 4ptj:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Ensemble Model For Escherichia Coli Dihydrofolate Reductase at 277K


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Ensemble Model For Escherichia Coli Dihydrofolate Reductase at 277K within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn203 b:14.0 occ:0.01 O A:HOH366 2.2 14.8 0.0 O A:ASP116 2.2 13.1 0.0 ND1 A:HIS149 2.3 13.5 0.0 CE1 A:HIS149 3.1 13.7 0.0 HE1 A:HIS149 3.1 13.9 0.0 HA A:ALA117 3.2 13.1 0.0 C A:ASP116 3.4 12.7 0.0 CG A:HIS149 3.4 13.1 0.0 HB3 A:HIS149 3.4 12.9 0.0 HA A:HIS149 3.7 13.8 0.0 CB A:HIS149 3.8 12.9 0.0 CA A:ALA117 3.9 12.7 0.0 N A:ALA117 4.1 12.5 0.0 HB2 A:ALA117 4.2 12.4 0.0 HB2 A:ASP116 4.2 13.0 0.0 HB3 A:ASP116 4.2 13.2 0.0 CA A:HIS149 4.3 13.5 0.0 NE2 A:HIS149 4.3 13.3 0.0 HB1 A:ALA117 4.4 12.7 0.0 CB A:ALA117 4.4 12.5 0.0 CD2 A:HIS149 4.5 13.0 0.0 H A:SER150 4.5 13.6 0.0 O A:HOH328 4.5 14.2 0.0 CB A:ASP116 4.5 12.9 0.0 CA A:ASP116 4.6 12.5 0.0 HB2 A:HIS149 4.7 12.6 0.0 O A:SER148 4.8 14.6 0.0 H A:GLU118 4.8 13.6 0.0 H A:ALA117 4.9 12.3 0.0

Manganese binding site 2 out of 2 in the Ensemble Model For Escherichia Coli Dihydrofolate Reductase at 277K


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Ensemble Model For Escherichia Coli Dihydrofolate Reductase at 277K within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn204 b:10.4 occ:0.01 HG A:LEU156 1.6 10.9 0.0 OE2 A:GLU154 2.1 11.1 0.0 CG A:LEU156 2.5 11.1 0.0 HD13 A:LEU112 2.6 10.2 0.0 CD A:GLU154 2.6 11.2 0.0 OE1 A:GLU154 2.7 11.2 0.0 HG A:LEU112 2.8 9.7 0.0 HD13 A:LEU156 2.8 10.6 0.0 HB2 A:LEU110 2.9 10.1 0.0 H A:LEU156 2.9 10.8 0.0 HB2 A:LEU156 2.9 10.9 0.0 CD1 A:LEU156 2.9 10.8 0.0 HD11 A:LEU156 3.0 10.8 0.0 O A:LEU110 3.1 10.2 0.0 CB A:LEU156 3.1 11.2 0.0 HB2 A:LEU112 3.2 10.0 0.0 N A:LEU156 3.2 11.1 0.0 CD1 A:LEU112 3.4 10.0 0.0 CG A:LEU112 3.4 9.7 0.0 O A:GLU154 3.4 10.4 0.0 HB3 A:GLU154 3.5 10.8 0.0 H A:LEU112 3.5 9.9 0.0 HA A:ILE155 3.6 10.7 0.0 CD2 A:LEU156 3.7 11.6 0.0 CB A:LEU110 3.7 9.9 0.0 CA A:LEU156 3.7 11.4 0.0 HB3 A:LEU110 3.7 9.7 0.0 C A:ILE155 3.8 11.3 0.0 CB A:LEU112 3.8 9.8 0.0 HD22 A:LEU156 3.8 11.8 0.0 C A:GLU154 3.8 10.8 0.0 C A:LEU110 3.9 9.9 0.0 HD12 A:LEU156 3.9 11.0 0.0 CG A:GLU154 3.9 11.4 0.0 HD12 A:LEU112 3.9 9.9 0.0 HD23 A:LEU156 4.0 11.6 0.0 HB3 A:LEU156 4.0 11.4 0.0 CA A:ILE155 4.0 11.0 0.0 N A:LEU112 4.0 9.7 0.0 HD11 A:LEU112 4.0 10.0 0.0 CB A:GLU154 4.1 11.1 0.0 HD12 A:LEU110 4.1 10.1 0.0 N A:ILE155 4.1 11.1 0.0 HA A:LEU156 4.3 11.7 0.0 HG2 A:GLU154 4.3 11.7 0.0 HA A:TYR111 4.4 9.9 0.0 CA A:LEU110 4.4 9.8 0.0 HD21 A:LEU156 4.5 11.8 0.0 CA A:LEU112 4.5 9.7 0.0 HD11 A:LEU110 4.5 10.4 0.0 HG3 A:GLU154 4.5 11.6 0.0 O A:ILE155 4.5 11.8 0.0 HB3 A:LEU112 4.6 9.8 0.0 CA A:GLU154 4.6 11.1 0.0 N A:TYR111 4.6 9.6 0.0 CD1 A:LEU110 4.7 10.2 0.0 H A:LEU110 4.7 10.4 0.0 H A:ILE155 4.8 11.4 0.0 CD2 A:LEU112 4.8 9.5 0.0 CG A:LEU110 4.8 10.0 0.0 C A:TYR111 4.8 9.6 0.0 HD21 A:LEU112 4.8 9.4 0.0 CA A:TYR111 4.8 9.7 0.0 C A:LEU156 4.9 11.4 0.0 HB2 A:GLU154 4.9 11.3 0.0 O A:LEU156 5.0 11.0 0.0

D.A.Keedy, H.Van Den Bedem, D.A.Sivak, G.A.Petsko, D.Ringe, M.A.Wilson, J.S.Fraser. Crystal Cryocooling Distorts Conformational Heterogeneity in A Model Michaelis Complex of Dhfr. Structure V. 22 899 2014.
ISSN: ISSN 0969-2126
PubMed: 24882744
DOI: 10.1016/J.STR.2014.04.016