Manganese in PDB 4pss: Multiconformer Model For Escherichia Coli Dihydrofolate Reductase at 100K

The structure of Multiconformer Model For Escherichia Coli Dihydrofolate Reductase at 100K, PDB code: 4pss 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)	40.78 / 0.85
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	33.960, 44.823, 98.254, 90.00, 90.00, 90.00
R / Rfree (%)	15.3 / 16.9

The binding sites of Manganese atom in the Multiconformer Model For Escherichia Coli Dihydrofolate Reductase at 100K (pdb code 4pss). 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 100K, PDB code: 4pss:
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 100K


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 100K within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn203 b:38.4 occ:1.00 ND1 A:HIS149 2.0 8.8 0.3 O A:HOH588 2.0 21.1 1.0 O A:ASP116 2.2 6.7 0.6 O A:ASP116 2.2 6.7 0.4 O A:HOH572 2.3 9.7 1.0 O A:HOH573 2.5 34.6 1.0 ND1 A:HIS149 2.5 9.2 0.7 CE1 A:HIS149 2.6 9.4 0.3 HE1 A:HIS149 2.6 9.4 0.3 HA A:ALA117 3.0 7.3 0.6 HA A:ALA117 3.1 7.3 0.4 CG A:HIS149 3.2 8.8 0.3 CE1 A:HIS149 3.3 10.5 0.7 C A:ASP116 3.3 6.3 0.6 HE1 A:HIS149 3.4 9.4 0.7 C A:ASP116 3.4 6.6 0.4 HA A:HIS149 3.4 7.7 0.7 HB3 A:HIS149 3.5 8.9 0.7 CG A:HIS149 3.5 7.9 0.7 HB3 A:HIS149 3.6 8.9 0.3 HA A:HIS149 3.8 7.7 0.3 NE2 A:HIS149 3.8 9.7 0.3 HB2 A:ALA117 3.8 8.3 0.6 CB A:HIS149 3.9 8.9 0.3 CB A:HIS149 3.9 7.4 0.7 CA A:ALA117 3.9 8.2 0.6 CA A:ALA117 4.0 7.3 0.4 N A:ALA117 4.0 6.8 0.6 O A:HOH464 4.1 23.9 1.0 HB3 A:ASP116 4.1 6.9 0.6 HB2 A:ASP116 4.1 6.9 0.4 CD2 A:HIS149 4.1 9.6 0.3 N A:ALA117 4.1 6.7 0.4 HB3 A:ASP116 4.2 6.9 0.4 CA A:HIS149 4.2 6.3 0.7 HB2 A:ASP116 4.2 6.9 0.6 HB2 A:ALA117 4.3 8.3 0.4 H A:SER150 4.3 7.1 0.7 CB A:ALA117 4.4 8.7 0.6 H A:SER150 4.4 7.1 0.3 CA A:HIS149 4.4 7.7 0.3 NE2 A:HIS149 4.5 10.1 0.7 CB A:ASP116 4.5 6.6 0.6 CA A:ASP116 4.5 6.0 0.6 CB A:ASP116 4.5 6.9 0.4 O A:SER148 4.5 9.3 0.3 CA A:ASP116 4.6 6.4 0.4 O A:SER148 4.6 10.2 0.4 CD2 A:HIS149 4.6 9.7 0.7 HE2 A:HIS149 4.6 9.7 0.3 CB A:ALA117 4.7 8.3 0.4 HB1 A:ALA117 4.7 8.3 0.6 H A:GLU118 4.7 8.0 0.4 H A:GLU118 4.8 8.0 0.6 O A:HOH617 4.8 31.3 1.0 HB2 A:HIS149 4.9 8.9 0.3 HB2 A:HIS149 4.9 8.9 0.7 HB1 A:ALA117 5.0 8.3 0.4

Manganese binding site 2 out of 2 in the Multiconformer Model For Escherichia Coli Dihydrofolate Reductase at 100K


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 100K within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn204 b:33.1 occ:1.00 O A:HOH566 2.1 15.2 1.0 O A:HOH567 2.2 16.1 1.0 O A:HOH570 2.2 15.7 1.0 O A:HOH568 2.2 20.3 1.0 O A:HOH569 2.2 14.6 1.0 OE2 A:GLU154 2.2 9.8 1.0 CD A:GLU154 3.1 8.2 1.0 O A:HOH344 3.2 11.4 1.0 HB2 A:SER135 3.3 10.2 1.0 OE1 A:GLU154 3.4 9.2 1.0 HG A:SER135 3.5 9.7 1.0 HD21 A:LEU156 3.5 12.2 0.5 HD21 A:LEU156 3.9 12.2 0.5 CB A:SER135 4.1 10.2 1.0 OG A:SER135 4.2 9.7 1.0 O A:HOH438 4.3 13.6 1.0 O A:HOH561 4.4 12.9 1.0 HE2 A:HIS114 4.4 6.4 0.2 HB3 A:SER135 4.5 10.2 1.0 CD2 A:LEU156 4.5 9.3 0.5 CG A:GLU154 4.5 9.2 1.0 O A:HOH403 4.6 18.2 1.0 O A:HOH354 4.6 18.5 1.0 HD23 A:LEU156 4.6 12.2 0.5 HE2 A:HIS114 4.6 6.4 0.2 HG3 A:GLU154 4.7 9.2 1.0 HE2 A:HIS114 4.7 6.4 0.3 HE2 A:HIS114 4.7 6.4 0.3 HD23 A:LEU156 4.8 12.2 0.5 CD2 A:LEU156 4.8 12.2 0.5 HD11 A:LEU156 5.0 14.0 0.5

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