Manganese in PDB 3ql3: Re-Refined Coordinates For Pdb Entry 1RX2

All present enzymatic activity of Re-Refined Coordinates For Pdb Entry 1RX2:
1.5.1.3;

The structure of Re-Refined Coordinates For Pdb Entry 1RX2, PDB code: 3ql3 was solved by G.Bhabha, D.C.Ekiert, P.E.Wright, I.A.Wilson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	41.00 / 1.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	34.320, 45.510, 98.910, 90.00, 90.00, 90.00
R / Rfree (%)	17.7 / 21.3

The binding sites of Manganese atom in the Re-Refined Coordinates For Pdb Entry 1RX2 (pdb code 3ql3). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Re-Refined Coordinates For Pdb Entry 1RX2, PDB code: 3ql3:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Re-Refined Coordinates For Pdb Entry 1RX2


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Re-Refined Coordinates For Pdb Entry 1RX2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn162 b:23.8 occ:1.00 O A:ASP116 2.3 17.1 0.4 O A:ASP116 2.3 16.8 0.6 ND1 A:HIS149 2.4 22.2 1.0 O A:HOH166 2.4 13.8 1.0 CE1 A:HIS149 3.2 24.9 1.0 C A:ASP116 3.4 16.5 0.4 CG A:HIS149 3.4 17.1 1.0 C A:ASP116 3.5 16.6 0.6 CB A:HIS149 3.8 14.7 1.0 CA A:ALA117 4.0 18.0 1.0 N A:ALA117 4.1 16.3 1.0 OD2 A:ASP116 4.2 20.3 0.4 CG A:ASP116 4.3 18.5 0.4 NE2 A:HIS149 4.3 22.5 1.0 CA A:HIS149 4.4 15.1 1.0 CB A:ASP116 4.5 16.8 0.4 CD2 A:HIS149 4.5 19.2 1.0 CB A:ALA117 4.6 17.6 1.0 CA A:ASP116 4.6 15.2 0.4 CB A:ASP116 4.6 16.9 0.6 CA A:ASP116 4.6 15.3 0.6 O A:SER148 4.8 18.0 1.0 OD1 A:ASP116 4.9 20.2 0.4

Manganese binding site 2 out of 2 in the Re-Refined Coordinates For Pdb Entry 1RX2


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Re-Refined Coordinates For Pdb Entry 1RX2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn163 b:33.1 occ:1.00 OD2 A:ASP70 2.5 27.5 1.0 CG A:ASP70 3.3 20.5 1.0 O A:HOH194 3.7 26.8 1.0 OD1 A:ASP70 3.7 20.4 1.0 CB A:ASP70 4.5 19.1 1.0

G.Bhabha, J.Lee, D.C.Ekiert, J.Gam, I.A.Wilson, H.J.Dyson, S.J.Benkovic, P.E.Wright. A Dynamic Knockout Reveals That Conformational Fluctuations Influence the Chemical Step of Enzyme Catalysis. Science V. 332 234 2011.
ISSN: ISSN 0036-8075
PubMed: 21474759
DOI: 10.1126/SCIENCE.1198542