Manganese in PDB 2nrz: Crystal Structure of the C-Terminal Half of Uvrc Bound to Its Catalytic Divalent Cation

The structure of Crystal Structure of the C-Terminal Half of Uvrc Bound to Its Catalytic Divalent Cation, PDB code: 2nrz was solved by E.Karakas, J.J.Truglio, C.Kisker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.00 / 2.00
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	35.395, 83.853, 100.642, 90.00, 99.49, 90.00
R / Rfree (%)	18.3 / 23.4

The binding sites of Manganese atom in the Crystal Structure of the C-Terminal Half of Uvrc Bound to Its Catalytic Divalent Cation (pdb code 2nrz). 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 the C-Terminal Half of Uvrc Bound to Its Catalytic Divalent Cation, PDB code: 2nrz:
Jump to Manganese binding site number: 1; 2; 3;

Manganese binding site 1 out of 3 in the Crystal Structure of the C-Terminal Half of Uvrc Bound to Its Catalytic Divalent Cation


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 the C-Terminal Half of Uvrc Bound to Its Catalytic Divalent Cation within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn301 b:38.0 occ:1.00 O B:HOH195 2.2 40.7 1.0 OD2 B:ASP385 2.2 23.4 1.0 OD1 B:ASP385 2.4 32.0 1.0 O A:HOH3 2.4 25.6 1.0 OD2 A:ASP385 2.4 29.9 1.0 CG B:ASP385 2.6 30.6 1.0 CG A:ASP385 3.1 30.1 1.0 OD1 A:ASP385 3.2 28.0 1.0 CB B:ASP385 4.1 30.9 1.0 CE1 B:TYR361 4.4 22.5 1.0 O B:HOH28 4.5 34.8 1.0 O A:HOH15 4.5 34.0 1.0 O B:HOH129 4.5 53.0 1.0 OH B:TYR361 4.5 23.0 1.0 CB A:ASP385 4.5 30.7 1.0 CD A:LYS344 4.5 31.6 1.0 NZ A:LYS344 4.7 33.1 1.0

Manganese binding site 2 out of 3 in the Crystal Structure of the C-Terminal Half of Uvrc Bound to Its Catalytic Divalent Cation


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 the C-Terminal Half of Uvrc Bound to Its Catalytic Divalent Cation within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn303 b:44.3 occ:0.60 O A:HOH116 2.2 56.8 1.0 O A:HOH193 2.3 35.4 1.0 O A:HOH186 2.3 38.2 1.0 O A:HOH198 2.4 57.2 1.0 ND1 A:HIS488 2.4 39.8 1.0 O A:HOH113 2.7 48.6 1.0 CG A:HIS488 3.3 34.8 1.0 CE1 A:HIS488 3.3 39.3 1.0 CB A:HIS488 3.5 32.2 1.0 OD2 A:ASP429 3.8 35.9 1.0 OD1 A:ASP367 3.9 41.6 1.0 CA A:HIS488 4.3 31.4 1.0 O A:HOH207 4.3 52.8 1.0 CD2 A:HIS488 4.4 38.1 1.0 NE2 A:HIS488 4.4 38.9 1.0 O A:HOH176 4.5 50.7 1.0 CG A:ASP429 4.7 34.0 1.0 OD1 A:ASP429 4.8 33.0 1.0

Manganese binding site 3 out of 3 in the Crystal Structure of the C-Terminal Half of Uvrc Bound to Its Catalytic Divalent Cation


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 the C-Terminal Half of Uvrc Bound to Its Catalytic Divalent Cation within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn302 b:45.6 occ:0.80 O B:HOH196 2.0 46.9 1.0 ND1 B:HIS488 2.0 35.9 1.0 O B:HOH49 2.2 36.0 1.0 O B:HOH174 2.4 47.1 1.0 O B:HOH169 2.7 58.9 1.0 CE1 B:HIS488 2.9 36.5 1.0 CG B:HIS488 3.0 33.8 1.0 CB B:HIS488 3.5 32.2 1.0 OD1 B:ASP367 3.7 37.3 1.0 NE2 B:HIS488 4.0 37.2 1.0 CD2 B:HIS488 4.1 35.3 1.0 O B:HOH88 4.1 42.5 1.0 CA B:HIS488 4.1 31.9 1.0 OD2 B:ASP429 4.2 38.7 1.0 CG B:ASP367 4.8 34.6 1.0 CG B:ASP429 4.9 38.1 1.0 OD1 B:ASP429 5.0 38.9 1.0 N B:HIS488 5.0 31.1 1.0

E.Karakas, J.J.Truglio, D.Croteau, B.Rhau, L.Wang, B.Van Houten, C.Kisker. Structure of the C-Terminal Half of Uvrc Reveals An Rnase H Endonuclease Domain with An Argonaute-Like Catalytic Triad. Embo J. V. 26 613 2007.
ISSN: ISSN 0261-4189
PubMed: 17245438
DOI: 10.1038/SJ.EMBOJ.7601497