Zinc in PDB 5lb8: Crystal Structure of Human RECQL5 Helicase Apo Form.

All present enzymatic activity of Crystal Structure of Human RECQL5 Helicase Apo Form.:
3.6.4.12;

The structure of Crystal Structure of Human RECQL5 Helicase Apo Form., PDB code: 5lb8 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)	48.61 / 3.40
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	68.740, 68.740, 396.307, 90.00, 90.00, 90.00
R / Rfree (%)	30.1 / 32.2

The binding sites of Zinc atom in the Crystal Structure of Human RECQL5 Helicase Apo Form. (pdb code 5lb8). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Human RECQL5 Helicase Apo Form., PDB code: 5lb8:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Human RECQL5 Helicase Apo Form.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Human RECQL5 Helicase Apo Form. within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn601 b:0.1 occ:1.00 SG A:CYS411 2.2 0.5 1.0 CB A:CYS431 2.4 0.6 1.0 SG A:CYS434 2.5 0.2 1.0 SG A:CYS431 2.5 0.4 1.0 CB A:CYS411 3.2 0.8 1.0 CA A:CYS411 3.7 0.7 1.0 CA A:CYS431 3.9 0.4 1.0 CB A:CYS434 4.0 0.4 1.0 N A:ARG412 4.0 0.2 1.0 CB A:CYS427 4.0 0.8 1.0 N A:CYS434 4.2 0.7 1.0 SG A:CYS427 4.2 0.7 1.0 C A:CYS411 4.3 0.5 1.0 N A:CYS431 4.5 0.4 1.0 CB A:HIS433 4.5 0.3 1.0 C A:CYS431 4.6 0.3 1.0 N A:HIS413 4.6 0.3 1.0 CA A:CYS434 4.6 0.1 1.0 ND1 A:HIS413 4.7 0.9 1.0 C A:HIS433 4.9 0.8 1.0 N A:HIS433 4.9 0.1 1.0 CB A:HIS413 5.0 0.1 1.0 O A:CYS431 5.0 0.8 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Human RECQL5 Helicase Apo Form.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Human RECQL5 Helicase Apo Form. within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn601 b:0.5 occ:1.00 SG D:CYS411 2.2 0.5 1.0 SG D:CYS434 2.4 0.4 1.0 CB D:CYS431 2.6 0.5 1.0 SG D:CYS431 3.0 0.3 1.0 CB D:CYS411 3.4 0.7 1.0 CB D:CYS427 3.5 0.2 1.0 SG D:CYS427 3.8 0.2 1.0 CB D:CYS434 3.9 0.4 1.0 CA D:CYS431 4.1 0.3 1.0 CA D:CYS411 4.1 0.5 1.0 N D:ARG412 4.3 0.4 1.0 N D:CYS434 4.5 0.2 1.0 ND1 D:HIS413 4.5 0.2 1.0 N D:CYS431 4.5 0.0 1.0 C D:CYS411 4.6 0.5 1.0 CA D:CYS427 4.6 0.7 1.0 N D:HIS413 4.6 1.0 1.0 O D:CYS427 4.7 0.4 1.0 C D:CYS427 4.7 0.2 1.0 CA D:CYS434 4.7 0.0 1.0 CB D:HIS413 4.8 0.3 1.0 C D:CYS431 4.8 0.5 1.0 C D:GLY430 4.9 0.4 1.0 CB D:HIS433 5.0 0.9 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