Manganese in PDB 8uw0: Escherichia Coli Dhfr Bound to Nadp+ and Folate, 17.2 Mgy Dose

The structure of Escherichia Coli Dhfr Bound to Nadp+ and Folate, 17.2 Mgy Dose, PDB code: 8uw0 was solved by N.Smith, A.R.Horswill, M.A.Wilson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.12 / 0.93
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	33.98, 44.848, 98.24, 90, 90, 90
R / Rfree (%)	10 / 11.5

The binding sites of Manganese atom in the Escherichia Coli Dhfr Bound to Nadp+ and Folate, 17.2 Mgy Dose (pdb code 8uw0). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 4 binding sites of Manganese where determined in the Escherichia Coli Dhfr Bound to Nadp+ and Folate, 17.2 Mgy Dose, PDB code: 8uw0:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in the Escherichia Coli Dhfr Bound to Nadp+ and Folate, 17.2 Mgy Dose


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Escherichia Coli Dhfr Bound to Nadp+ and Folate, 17.2 Mgy Dose within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn203 b:7.2 occ:0.60 ND1 A:HIS149 1.9 13.6 0.3 O A:HOH500 2.0 20.6 1.0 O A:ASP116 2.1 7.4 1.0 O A:HOH477 2.1 20.4 1.0 O A:HOH476 2.3 9.0 1.0 ND1 A:HIS149 2.3 8.4 0.7 CE1 A:HIS149 2.5 14.6 0.3 HE1 A:HIS149 2.5 17.5 0.3 CG A:HIS149 3.1 13.6 0.3 HA A:ALA117 3.1 9.0 1.0 CE1 A:HIS149 3.2 9.0 0.7 HE1 A:HIS149 3.2 10.8 0.7 C A:ASP116 3.3 6.1 1.0 HB3 A:HIS149 3.4 8.0 0.7 CG A:HIS149 3.4 7.0 0.7 HB3 A:HIS149 3.5 13.5 0.3 HA A:HIS149 3.5 7.4 0.7 HA A:HIS149 3.7 11.2 0.3 NE2 A:HIS149 3.7 15.5 0.3 CB A:HIS149 3.7 11.3 0.3 CB A:HIS149 3.8 6.7 0.7 CA A:ALA117 3.9 7.5 1.0 CD2 A:HIS149 4.0 15.8 0.3 N A:ALA117 4.1 6.6 1.0 HB3 A:ASP116 4.1 7.5 1.0 HB2 A:ALA117 4.1 10.9 1.0 CA A:HIS149 4.2 6.1 0.7 O A:HOH505 4.2 14.6 1.0 HB2 A:ASP116 4.2 7.5 1.0 O A:HOH536 4.2 20.6 1.0 CA A:HIS149 4.2 9.3 0.3 O A:HOH554 4.3 22.2 0.8 NE2 A:HIS149 4.4 9.4 0.7 O A:SER148 4.4 11.7 0.3 H A:SER150 4.4 8.2 0.7 HE2 A:HIS149 4.5 18.6 0.3 H A:SER150 4.5 8.2 0.3 CB A:ASP116 4.5 6.3 1.0 CA A:ASP116 4.5 5.9 1.0 CD2 A:HIS149 4.5 8.5 0.7 CB A:ALA117 4.6 9.1 1.0 HB2 A:HIS149 4.6 13.5 0.3 HB2 A:HIS149 4.7 8.0 0.7 H A:GLU118 4.8 9.6 0.5 O A:SER148 4.8 10.7 0.7 HB1 A:ALA117 4.8 10.9 1.0 H A:GLU118 4.9 9.9 0.5 H A:ALA117 4.9 8.0 1.0 HD2 A:HIS149 4.9 19.0 0.3

Manganese binding site 2 out of 4 in the Escherichia Coli Dhfr Bound to Nadp+ and Folate, 17.2 Mgy Dose


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Escherichia Coli Dhfr Bound to Nadp+ and Folate, 17.2 Mgy Dose within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn204 b:7.9 occ:0.47 O A:HOH519 2.1 13.9 0.8 O A:HOH509 2.1 12.3 0.6 O A:HOH547 2.2 11.8 0.7 O A:HOH637 2.2 15.3 0.8 OE2 A:GLU154 2.3 9.9 1.0 O A:HOH340 2.3 13.0 0.8 CD A:GLU154 3.2 8.1 1.0 O A:HOH625 3.2 8.3 0.8 HB2 A:SER135 3.3 10.8 1.0 OE1 A:GLU154 3.4 8.7 1.0 HD21 A:LEU156 3.7 10.1 0.6 CB A:SER135 4.1 9.0 1.0 OG A:SER135 4.2 9.6 1.0 HG A:SER135 4.2 11.5 1.0 O A:HOH327 4.2 22.3 0.7 O A:HOH383 4.3 15.3 1.0 HD21 A:LEU156 4.4 18.5 0.4 HB3 A:SER135 4.4 10.8 1.0 CD2 A:LEU156 4.5 8.4 0.6 CG A:GLU154 4.5 8.1 1.0 HD23 A:LEU156 4.6 10.1 0.6 O A:HOH471 4.6 18.7 1.0 HG3 A:GLU154 4.6 9.7 1.0 HE2 A:HIS114 4.7 7.0 0.5 HE2 A:HIS114 4.8 12.4 0.5 O A:HOH565 4.8 28.6 0.7 HG A:LEU156 5.0 14.4 0.4 HG2 A:GLU154 5.0 9.7 1.0

Manganese binding site 3 out of 4 in the Escherichia Coli Dhfr Bound to Nadp+ and Folate, 17.2 Mgy Dose


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Escherichia Coli Dhfr Bound to Nadp+ and Folate, 17.2 Mgy Dose within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn205 b:6.4 occ:0.32 HB3 A:SER138 1.7 18.6 0.5 O A:SER138 2.1 11.4 0.5 O A:HOH503 2.1 20.6 1.0 OG A:SER138 2.2 8.5 0.5 O A:HOH464 2.2 25.6 1.0 O A:HOH405 2.2 19.5 0.9 OG A:SER138 2.4 18.5 0.5 CB A:SER138 2.4 15.5 0.5 HB2 A:SER138 3.0 18.6 0.5 CB A:SER138 3.1 7.8 0.5 C A:SER138 3.1 8.7 0.5 HB2 A:SER138 3.2 9.3 0.5 O A:SER138 3.3 11.0 0.5 C A:SER138 3.4 10.2 0.5 CA A:SER138 3.4 11.7 0.5 CA A:SER138 3.5 7.2 0.5 H A:SER138 3.9 8.5 0.5 HB3 A:SER138 3.9 9.3 0.5 O A:HOH327 3.9 22.3 0.7 H A:SER138 4.0 12.7 0.5 N A:SER138 4.1 7.1 0.5 HA A:SER138 4.1 14.1 0.5 O A:HOH486 4.1 12.4 1.0 N A:SER138 4.1 10.6 0.5 N A:GLU139 4.2 8.1 1.0 O A:HOH391 4.3 25.6 1.0 HA A:GLU139 4.4 9.9 1.0 HA A:SER138 4.4 8.7 0.5 O A:HOH357 4.6 26.6 1.0 OD2 A:OCS152 4.6 12.0 1.0 H A:GLU139 4.7 9.8 0.5 CA A:GLU139 4.8 8.3 1.0 H A:PHE140 4.9 9.0 1.0 H A:GLU139 4.9 9.8 0.5

Manganese binding site 4 out of 4 in the Escherichia Coli Dhfr Bound to Nadp+ and Folate, 17.2 Mgy Dose


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Escherichia Coli Dhfr Bound to Nadp+ and Folate, 17.2 Mgy Dose within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn206 b:17.5 occ:0.47 O A:HOH596 2.0 28.8 1.0 O A:HOH661 2.1 30.4 1.0 O A:HOH370 2.1 16.8 0.9 O A:HOH615 3.0 14.1 0.6 O A:HOH301 3.1 10.8 0.7 OE1 A:GLU129 3.8 16.3 0.4 HD2 A:PRO130 3.8 10.3 0.6 HD2 A:PRO130 3.9 11.8 0.4 OE2 A:GLU129 4.3 15.0 0.4 HG3 A:PRO130 4.3 11.3 0.6 O A:HOH452 4.4 21.9 0.6 HG2 A:PRO130 4.4 11.3 0.6 CD A:GLU129 4.4 14.8 0.4 OE2 A:GLU129 4.5 9.2 0.6 OE1 A:GLU129 4.5 10.9 0.6 O A:HOH641 4.5 36.1 1.0 CD A:PRO130 4.5 8.6 0.6 CG A:PRO130 4.6 9.4 0.6 HG2 A:PRO130 4.7 13.2 0.4 HD3 A:PRO130 4.7 10.3 0.6 CD A:PRO130 4.7 9.8 0.4 CD A:GLU129 4.9 9.4 0.6 HG3 A:PRO130 4.9 13.2 0.4

N.Smith, A.R.Horswill, M.A.Wilson. X-Ray-Driven Chemistry and Conformational Heterogeneity in Atomic Resolution Crystal Structures of Bacterial Dihydrofolate Reductases To Be Published.