Manganese in PDB 5hwu: Crystal Structure of DR2231_E46A Mutant in Complex with Dumpnpp and Manganese

The structure of Crystal Structure of DR2231_E46A Mutant in Complex with Dumpnpp and Manganese, PDB code: 5hwu was solved by C.S.Mota, A.M.D.Goncalves, D.De Sanctis, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	41.52 / 2.10
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	52.263, 78.014, 141.958, 90.00, 90.00, 90.00
R / Rfree (%)	20.1 / 24.7

The binding sites of Manganese atom in the Crystal Structure of DR2231_E46A Mutant in Complex with Dumpnpp and Manganese (pdb code 5hwu). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 3 binding sites of Manganese where determined in the Crystal Structure of DR2231_E46A Mutant in Complex with Dumpnpp and Manganese, PDB code: 5hwu:
Jump to Manganese binding site number: 1; 2; 3;

Manganese binding site 1 out of 3 in the Crystal Structure of DR2231_E46A Mutant in Complex with Dumpnpp and Manganese


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of DR2231_E46A Mutant in Complex with Dumpnpp and Manganese within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn201 b:33.4 occ:1.00 OE1 A:GLU50 2.1 31.1 1.0 OD2 A:ASP82 2.1 18.7 1.0 OE1 A:GLU47 2.2 33.7 1.0 OE1 A:GLU79 2.3 29.2 1.0 O A:HOH315 2.5 26.9 1.0 O A:HOH331 2.6 37.4 1.0 CD A:GLU79 3.1 23.9 1.0 CD A:GLU47 3.1 30.7 1.0 CG A:ASP82 3.2 21.9 1.0 CD A:GLU50 3.2 36.6 1.0 OE2 A:GLU79 3.2 24.3 1.0 OE2 A:GLU47 3.3 28.6 1.0 CB A:ASP82 3.5 18.6 1.0 OE2 A:GLU50 3.7 44.2 1.0 CG A:GLU50 4.3 34.3 1.0 OD1 A:ASP82 4.3 22.6 1.0 CB A:GLU50 4.4 29.1 1.0 CG A:GLU79 4.6 22.3 1.0 CG A:GLU47 4.6 25.7 1.0 O A:HOH338 4.7 30.9 1.0 CA A:GLU79 4.8 28.0 1.0 CB A:GLU79 5.0 22.8 1.0

Manganese binding site 2 out of 3 in the Crystal Structure of DR2231_E46A Mutant in Complex with Dumpnpp and Manganese


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of DR2231_E46A Mutant in Complex with Dumpnpp and Manganese within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn202 b:21.0 occ:1.00 OE1 B:GLU79 2.1 27.3 1.0 OE1 B:GLU50 2.1 29.8 1.0 OD2 B:ASP82 2.2 16.9 1.0 O B:HOH309 2.2 22.7 1.0 OE1 B:GLU47 2.3 22.5 1.0 O B:HOH305 2.4 23.4 1.0 CD B:GLU79 3.0 25.2 1.0 CG B:ASP82 3.2 15.2 1.0 CD B:GLU50 3.2 31.2 1.0 CD B:GLU47 3.2 22.5 1.0 OE2 B:GLU79 3.3 25.3 1.0 OE2 B:GLU47 3.5 20.8 1.0 CB B:ASP82 3.5 14.2 1.0 MN B:MN203 3.6 23.8 1.0 OE2 B:GLU50 3.8 36.3 1.0 O2B B:DUP201 3.8 20.4 1.0 CB B:GLU50 4.2 25.0 1.0 CG B:GLU50 4.3 28.5 1.0 OD1 B:ASP82 4.3 18.1 1.0 O1G B:DUP201 4.4 20.1 1.0 CG B:GLU79 4.5 23.0 1.0 CG B:GLU47 4.6 18.4 1.0 NE2 B:HIS78 4.7 32.3 1.0 O B:HOH342 4.7 26.9 1.0 CA B:GLU79 4.8 16.9 1.0 CB B:GLU79 4.9 16.8 1.0 CA B:GLU47 4.9 21.0 1.0 CB B:GLU47 5.0 19.0 1.0

Manganese binding site 3 out of 3 in the Crystal Structure of DR2231_E46A Mutant in Complex with Dumpnpp and Manganese


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Crystal Structure of DR2231_E46A Mutant in Complex with Dumpnpp and Manganese within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn203 b:23.8 occ:1.00 O B:HOH309 2.0 22.7 1.0 O B:HOH341 2.0 20.2 1.0 NE2 B:HIS78 2.3 32.3 1.0 O3G B:DUP201 2.3 19.1 1.0 O2B B:DUP201 2.4 20.4 1.0 OD2 B:ASP82 2.5 16.9 1.0 CE1 B:HIS78 3.0 31.8 1.0 PG B:DUP201 3.2 25.6 1.0 CG B:ASP82 3.3 15.2 1.0 OD1 B:ASP82 3.4 18.1 1.0 CD2 B:HIS78 3.4 29.6 1.0 O B:HOH312 3.4 34.3 1.0 O1G B:DUP201 3.4 20.1 1.0 PB B:DUP201 3.5 24.9 1.0 MN B:MN202 3.6 21.0 1.0 O B:HOH305 3.7 23.4 1.0 O3B B:DUP201 3.7 26.5 1.0 O B:HOH311 3.9 27.0 1.0 O1B B:DUP201 4.1 23.7 1.0 ND1 B:HIS78 4.1 31.8 1.0 CG B:HIS78 4.4 27.9 1.0 OE2 B:GLU79 4.4 25.3 1.0 O2G B:DUP201 4.6 29.5 1.0 OE1 B:GLU79 4.6 27.3 1.0 CB B:ASP82 4.7 14.2 1.0 N3A B:DUP201 4.8 26.6 1.0 CD B:GLU79 4.9 25.2 1.0 C4' B:DUP201 5.0 20.9 1.0

C.S.Mota, A.M.Goncalves, D.De Sanctis. Deinococcus Radiodurans DR2231 Is A Two-Metal-Ion Mechanism Hydrolase with Exclusive Activity on Dutp. Febs J. V. 283 4274 2016.
ISSN: ISSN 1742-4658
PubMed: 27739259
DOI: 10.1111/FEBS.13923