Manganese in PDB 1oyy: Structure of the Recq Catalytic Core Bound to Atp-Gamma-S

The structure of Structure of the Recq Catalytic Core Bound to Atp-Gamma-S, PDB code: 1oyy was solved by D.A.Bernstein, M.C.Zittel, J.L.Keck, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.50
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	66.591, 54.534, 78.686, 90.00, 110.78, 90.00
R / Rfree (%)	21 / 29.8

The structure of Structure of the Recq Catalytic Core Bound to Atp-Gamma-S also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Manganese atom in the Structure of the Recq Catalytic Core Bound to Atp-Gamma-S (pdb code 1oyy). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Structure of the Recq Catalytic Core Bound to Atp-Gamma-S, PDB code: 1oyy:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Structure of the Recq Catalytic Core Bound to Atp-Gamma-S


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Structure of the Recq Catalytic Core Bound to Atp-Gamma-S within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn525 b:83.7 occ:1.00 OD2 A:ASP35 2.2 51.8 1.0 OE2 A:GLU10 2.3 0.9 1.0 OE1 A:GLU10 2.5 0.2 1.0 CD A:GLU10 2.8 0.8 1.0 OE2 A:GLU31 3.0 78.2 1.0 CG A:ASP35 3.2 51.4 1.0 OD1 A:ASP35 3.5 45.5 1.0 CG A:GLU31 3.6 66.7 1.0 CD A:GLU31 3.7 72.2 1.0 CG A:GLU10 4.3 98.9 1.0 O A:GLU10 4.4 80.2 1.0 CB A:ASP35 4.4 46.3 1.0 OE1 A:GLU31 4.7 69.6 1.0 CB A:GLU31 4.9 61.1 1.0

Manganese binding site 2 out of 2 in the Structure of the Recq Catalytic Core Bound to Atp-Gamma-S


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Structure of the Recq Catalytic Core Bound to Atp-Gamma-S within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn526 b:69.6 occ:1.00 O A:HOH529 2.2 56.6 1.0 O A:HOH568 2.4 74.3 1.0 O2B A:AGS527 2.4 76.1 1.0 O A:HOH528 2.4 66.7 1.0 O3G A:AGS527 3.1 98.5 1.0 PB A:AGS527 3.4 69.8 1.0 O3B A:AGS527 3.5 81.7 1.0 O3A A:AGS527 3.9 78.2 1.0 PG A:AGS527 4.0 94.8 1.0 O1A A:AGS527 4.0 65.1 1.0 OG A:SER54 4.1 65.6 1.0 PA A:AGS527 4.3 73.2 1.0 OD2 A:ASP146 4.4 59.2 1.0 O2A A:AGS527 4.4 68.3 1.0 CB A:LYS53 4.4 50.5 1.0 CE A:LYS53 4.5 83.6 1.0 OD1 A:ASP146 4.5 51.3 1.0 O1B A:AGS527 4.6 75.0 1.0 S1G A:AGS527 4.7 94.6 1.0 N A:SER54 4.8 56.4 1.0 CG A:ASP146 4.8 57.1 1.0 NZ A:LYS53 5.0 84.1 1.0 OE2 A:GLU147 5.0 57.1 1.0

D.A.Bernstein, M.C.Zittel, J.L.Keck. High-Resolution Structure of the E. Coli Recq Helicase Catalytic Core Embo J. V. 22 4910 2003.
ISSN: ISSN 0261-4189
PubMed: 14517231
DOI: 10.1093/EMBOJ/CDG500