Magnesium in PDB 5lb3: Crystal Structure of Human RECQL5 Helicase in Complex with Adp/Mg.

All present enzymatic activity of Crystal Structure of Human RECQL5 Helicase in Complex with Adp/Mg.:
3.6.4.12;

The structure of Crystal Structure of Human RECQL5 Helicase in Complex with Adp/Mg., PDB code: 5lb3 was solved by J.A.Newman, H.Aitkenhead, P.Savitsky, T.Krojer, F.Von Delft, C.H.Arrowsmith, A.M.Edwards, C.Bountra, O.Gileadi, Structural Genomicsconsortium (Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.88 / 1.80
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	72.757, 62.943, 104.703, 90.00, 95.44, 90.00
R / Rfree (%)	19.5 / 23.4

The structure of Crystal Structure of Human RECQL5 Helicase in Complex with Adp/Mg. also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Magnesium atom in the Crystal Structure of Human RECQL5 Helicase in Complex with Adp/Mg. (pdb code 5lb3). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of Human RECQL5 Helicase in Complex with Adp/Mg., PDB code: 5lb3:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Human RECQL5 Helicase in Complex with Adp/Mg.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Human RECQL5 Helicase in Complex with Adp/Mg. within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg503 b:44.8 occ:1.00 O B:HOH770 1.9 53.0 1.0 O2B B:ADP502 2.0 35.4 1.0 O B:HOH824 2.1 39.8 1.0 O B:HOH656 2.1 38.7 1.0 O B:HOH631 2.7 40.8 1.0 O B:HOH662 2.7 45.4 1.0 PB B:ADP502 3.2 36.8 1.0 O3B B:ADP502 3.5 32.0 1.0 OG B:SER59 3.7 34.2 1.0 OE2 B:GLU158 4.0 47.2 1.0 O1B B:ADP502 4.2 33.9 1.0 NE2 B:GLN86 4.2 60.7 1.0 OD2 B:ASP157 4.2 38.7 1.0 OD1 B:ASP157 4.2 32.7 1.0 CE B:LYS58 4.3 28.4 1.0 O1A B:ADP502 4.3 34.6 1.0 O3A B:ADP502 4.3 34.2 1.0 O B:HOH836 4.3 28.5 1.0 O2A B:ADP502 4.4 40.1 1.0 PA B:ADP502 4.5 33.7 1.0 CB B:LYS58 4.6 29.3 1.0 CG B:ASP157 4.7 38.5 1.0 NZ B:LYS58 4.7 31.9 1.0 N B:SER59 4.8 29.7 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Human RECQL5 Helicase in Complex with Adp/Mg.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Human RECQL5 Helicase in Complex with Adp/Mg. within 5.0Å range: probe atom residue distance (Å) B Occ E:Mg503 b:46.4 occ:1.00 O E:HOH752 2.0 37.5 1.0 O E:HOH827 2.3 37.9 1.0 O3B E:ADP502 2.3 36.5 1.0 O E:HOH635 2.4 42.9 1.0 O E:HOH680 2.8 36.1 1.0 PB E:ADP502 3.6 30.9 1.0 OG E:SER59 3.7 33.3 1.0 O2B E:ADP502 3.9 33.4 1.0 OD2 E:ASP157 4.0 36.5 1.0 O2A E:ADP502 4.3 35.7 1.0 OD1 E:ASP157 4.3 32.5 1.0 O1A E:ADP502 4.5 33.9 1.0 CG E:ASP157 4.6 34.6 1.0 O1B E:ADP502 4.6 28.2 1.0 O3A E:ADP502 4.6 34.8 1.0 PA E:ADP502 4.6 31.9 1.0 CE E:LYS58 4.7 24.4 1.0 O E:HOH776 4.8 31.5 1.0 O E:HOH678 4.9 39.6 1.0 CB E:LYS58 4.9 27.9 1.0 N E:SER59 5.0 24.1 1.0

J.A.Newman, H.Aitkenhead, P.Savitsky, O.Gileadi. Insights Into the Recq Helicase Mechanism Revealed By the Structure of the Helicase Domain of Human RECQL5. Nucleic Acids Res. V. 45 4231 2017.
ISSN: ESSN 1362-4962
PubMed: 28100692
DOI: 10.1093/NAR/GKW1362