Manganese in PDB 4pst: Multiconformer Model For Escherichia Coli Dihydrofolate Reductase at 277 K

The structure of Multiconformer Model For Escherichia Coli Dihydrofolate Reductase at 277 K, PDB code: 4pst 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 (%)	12.1 / 14.2

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

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


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Multiconformer Model For Escherichia Coli Dihydrofolate Reductase at 277 K within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn203 b:14.1 occ:1.00 O A:ASP116 2.1 8.9 0.2 ND1 A:HIS149 2.1 15.8 0.6 O A:HOH463 2.1 38.5 1.0 O A:HOH459 2.2 25.4 1.0 O A:ASP116 2.2 9.6 0.4 O A:ASP116 2.3 9.8 0.2 O A:HOH396 2.3 14.1 1.0 O A:ASP116 2.4 12.0 0.3 ND1 A:HIS149 2.4 12.7 0.4 CE1 A:HIS149 2.8 17.5 0.6 HE1 A:HIS149 2.9 11.7 0.6 HA A:ALA117 2.9 11.9 0.2 HA A:ALA117 3.0 11.9 0.4 HA A:ALA117 3.1 11.9 0.3 HA A:ALA117 3.2 11.9 0.2 CG A:HIS149 3.2 14.9 0.6 CE1 A:HIS149 3.3 11.7 0.4 C A:ASP116 3.3 8.5 0.2 HB3 A:HIS149 3.3 11.6 0.6 HE1 A:HIS149 3.4 11.7 0.4 C A:ASP116 3.4 9.1 0.2 HB3 A:HIS149 3.4 11.6 0.4 C A:ASP116 3.4 9.0 0.4 C A:ASP116 3.5 11.4 0.3 CG A:HIS149 3.5 11.9 0.4 HA A:HIS149 3.5 11.6 0.4 HB2 A:ALA117 3.6 12.4 0.2 HA A:HIS149 3.6 11.6 0.6 CB A:HIS149 3.7 12.9 0.6 CA A:ALA117 3.8 10.6 0.2 HB3 A:ASP116 3.8 13.6 0.2 CB A:HIS149 3.8 11.6 0.4 CA A:ALA117 3.9 11.3 0.4 OD2 A:ASP116 3.9 16.7 0.3 HB2 A:ALA117 4.0 12.4 0.4 N A:ALA117 4.0 9.5 0.2 HB2 A:ASP116 4.0 13.6 0.2 HB3 A:ASP116 4.0 13.6 0.3 NE2 A:HIS149 4.0 18.9 0.6 CA A:ALA117 4.1 11.9 0.3 CA A:ALA117 4.1 9.9 0.2 N A:ALA117 4.1 10.5 0.4 N A:ALA117 4.1 9.2 0.2 CB A:ALA117 4.1 11.7 0.2 CG A:ASP116 4.2 15.7 0.3 HB3 A:ASP116 4.2 13.6 0.2 N A:ALA117 4.2 12.3 0.3 O A:HOH466 4.2 33.5 1.0 CA A:HIS149 4.2 11.6 0.4 CD2 A:HIS149 4.2 17.3 0.6 CA A:HIS149 4.3 11.5 0.6 CB A:ASP116 4.3 9.3 0.2 HB2 A:ASP116 4.3 13.6 0.4 HB2 A:ASP116 4.3 13.6 0.2 HB3 A:ASP116 4.4 13.6 0.4 HB2 A:ALA117 4.4 12.4 0.3 HB2 A:ALA117 4.4 12.4 0.2 CA A:ASP116 4.4 8.7 0.2 H A:SER150 4.4 11.8 0.6 HB1 A:ALA117 4.4 12.4 0.2 CB A:ALA117 4.4 12.2 0.4 CB A:ASP116 4.5 13.6 0.3 NE2 A:HIS149 4.5 12.7 0.4 H A:SER150 4.5 11.8 0.4 H A:GLU118 4.5 12.8 0.2 O A:SER148 4.5 15.4 0.4 CA A:ASP116 4.6 9.4 0.2 CD2 A:HIS149 4.6 12.7 0.4 CA A:ASP116 4.6 11.9 0.3 CB A:ASP116 4.6 9.4 0.2 CA A:ASP116 4.6 9.3 0.4 H A:GLU118 4.6 12.8 0.3 CB A:ASP116 4.7 9.3 0.4 OD1 A:ASP116 4.7 17.7 0.3 H A:GLU118 4.7 12.8 0.4 HB2 A:HIS149 4.7 11.6 0.6 CB A:ALA117 4.8 12.4 0.3 HB1 A:ALA117 4.8 12.4 0.4 CB A:ALA117 4.8 10.8 0.2 H A:GLU118 4.8 12.8 0.2 HB2 A:HIS149 4.9 11.6 0.4 HE2 A:HIS149 4.9 12.7 0.6 O A:SER148 4.9 13.8 0.6 H A:ALA117 5.0 12.3 0.2

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


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Multiconformer Model For Escherichia Coli Dihydrofolate Reductase at 277 K within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn204 b:30.4 occ:1.00 OE2 A:GLU154 2.3 17.0 1.0 O A:HOH462 2.5 48.4 1.0 O A:HOH460 2.8 34.8 1.0 HB2 A:SER135 3.1 12.6 0.2 HG A:SER135 3.1 12.8 0.3 HB2 A:SER135 3.1 12.6 0.3 CD A:GLU154 3.2 13.8 1.0 HG A:SER135 3.3 12.8 0.2 HB2 A:SER135 3.4 12.6 0.3 HB2 A:SER135 3.4 12.6 0.1 OE1 A:GLU154 3.4 16.6 1.0 HD21 A:LEU156 3.5 11.2 0.2 HD21 A:LEU156 3.6 11.2 0.8 HG A:SER135 3.7 12.8 0.3 OG A:SER135 3.8 13.4 0.2 CB A:SER135 3.8 12.4 0.2 CB A:SER135 3.9 13.5 0.3 OG A:SER135 3.9 14.6 0.3 HG A:SER135 3.9 12.8 0.1 HB3 A:SER135 4.0 12.6 0.2 HB3 A:SER135 4.2 12.6 0.3 CB A:SER135 4.3 12.6 0.1 CB A:SER135 4.3 12.3 0.3 O A:HOH390 4.4 28.8 1.0 OG A:SER135 4.4 13.4 0.3 HB3 A:SER135 4.5 12.6 0.1 CD2 A:LEU156 4.5 11.2 0.2 OG A:SER135 4.5 12.8 0.1 CG A:GLU154 4.6 13.0 1.0 HE2 A:HIS114 4.6 9.4 0.2 CD2 A:LEU156 4.6 17.2 0.8 HG3 A:GLU154 4.7 13.0 1.0 HD22 A:LEU156 4.7 11.2 0.2 HB3 A:SER135 4.8 12.6 0.3 HD23 A:LEU156 4.8 11.2 0.8 HE2 A:HIS114 4.8 9.4 0.4 HD11 A:LEU156 4.9 11.1 0.2 HD23 A:LEU156 4.9 11.2 0.2 HE2 A:HIS114 4.9 9.4 0.3

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