Zinc in PDB 7zmp: Crystal Structure of Human RECQL5 Helicase Apo Form in Complex with Engineered Nanobody (Gluebody) G3-055

All present enzymatic activity of Crystal Structure of Human RECQL5 Helicase Apo Form in Complex with Engineered Nanobody (Gluebody) G3-055:
3.6.4.12;

The structure of Crystal Structure of Human RECQL5 Helicase Apo Form in Complex with Engineered Nanobody (Gluebody) G3-055, PDB code: 7zmp was solved by M.Ye, M.Makola, J.A.Newman, M.Fairhead, E.Maclean, T.Krojer, H.Aitkenhead, C.Bountra, O.Gileadi, F.Von Delft, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	129.02 / 3.63
Space group	P 2 21 21
Cell size a, b, c (Å), α, β, γ (°)	89.109, 159.267, 220.04, 90, 90, 90
R / Rfree (%)	33.2 / 35.9

The binding sites of Zinc atom in the Crystal Structure of Human RECQL5 Helicase Apo Form in Complex with Engineered Nanobody (Gluebody) G3-055 (pdb code 7zmp). 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 in Complex with Engineered Nanobody (Gluebody) G3-055, PDB code: 7zmp:
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 in Complex with Engineered Nanobody (Gluebody) G3-055


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 in Complex with Engineered Nanobody (Gluebody) G3-055 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn501 b:138.7 occ:1.00 SG A:CYS427 2.1 111.3 1.0 SG A:CYS431 2.3 120.4 1.0 SG A:CYS411 2.4 128.0 1.0 O A:HOH617 2.8 113.1 1.0 CB A:CYS431 3.0 120.6 1.0 SG A:CYS434 3.3 192.7 1.0 CB A:CYS427 3.5 126.9 1.0 CB A:CYS434 3.5 176.8 1.0 CB A:CYS411 3.6 120.3 1.0 CA A:CYS411 3.7 124.0 1.0 N A:ARG412 3.8 118.9 1.0 CD2 A:HIS413 3.8 151.0 1.0 N A:CYS431 3.9 128.7 1.0 CA A:CYS431 4.0 121.7 1.0 C A:CYS411 4.1 128.5 1.0 N A:HIS413 4.2 121.4 1.0 C A:GLY430 4.2 141.0 1.0 CG A:HIS413 4.4 145.1 1.0 CB A:HIS413 4.5 131.4 1.0 N A:CYS434 4.5 145.1 1.0 O A:GLY430 4.6 144.4 1.0 CA A:CYS434 4.6 161.7 1.0 CA A:CYS427 4.7 143.7 1.0 C A:CYS431 4.7 119.5 1.0 NE2 A:HIS413 4.8 154.8 1.0 CA A:ARG412 4.8 118.1 1.0 O A:CYS431 4.9 125.9 1.0 N A:GLY430 5.0 158.9 1.0 CA A:GLY430 5.0 146.8 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Human RECQL5 Helicase Apo Form in Complex with Engineered Nanobody (Gluebody) G3-055


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 in Complex with Engineered Nanobody (Gluebody) G3-055 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn501 b:122.2 occ:1.00 SG B:CYS431 2.2 148.6 1.0 SG B:CYS427 2.3 120.4 1.0 SG B:CYS411 2.3 111.6 1.0 O B:HOH604 2.5 150.0 1.0 SG B:CYS434 3.0 181.1 1.0 CB B:CYS431 3.1 139.4 1.0 CB B:CYS434 3.3 174.4 1.0 CB B:CYS411 3.4 112.7 1.0 CA B:CYS411 3.5 112.3 1.0 CB B:CYS427 3.5 126.3 1.0 N B:ARG412 3.7 119.4 1.0 C B:CYS411 3.9 115.5 1.0 N B:CYS431 4.0 133.9 1.0 CA B:CYS431 4.1 132.4 1.0 CD2 B:HIS413 4.1 131.1 1.0 N B:CYS434 4.2 140.9 1.0 CA B:CYS434 4.4 165.2 1.0 N B:HIS413 4.4 132.4 1.0 C B:GLY430 4.5 136.8 1.0 C B:CYS431 4.7 122.9 1.0 CG B:HIS413 4.7 123.6 1.0 CB B:HIS413 4.8 123.8 1.0 CA B:CYS427 4.8 134.7 1.0 O B:CYS431 4.8 126.3 1.0 CA B:ARG412 4.8 134.4 1.0 O B:GLY430 4.8 141.2 1.0 N B:CYS411 4.8 122.3 1.0 O B:CYS411 5.0 134.3 1.0

M.Ye, M.Makola, J.A.Newman, M.Fairhead, E.Maclean, T.Krojer, N.D.Wright, L.Koekemoer, A.Thompson, G.A.Bezerra, G.Yi, H.Li, V.L.Rangel, D.Mamalis, H.Aitkenhead, R.J.C.Gilbert, K.Duerr, B.G.Davis, C.Bountra, O.Gileadi, F.Von Delft. Gluebodies Improve Crystal Reliability and Diversity Through Transferable Nanobody Mutations That Introduce Constitutive Crystal Contacts To Be Published.