Zinc in PDB 7zmo: Crystal Structure of Human RECQL5 Helicase Apo Form in Complex with Engineered Nanobody (Gluebody) G3-052

Enzymatic activity of Crystal Structure of Human RECQL5 Helicase Apo Form in Complex with Engineered Nanobody (Gluebody) G3-052

All present enzymatic activity of Crystal Structure of Human RECQL5 Helicase Apo Form in Complex with Engineered Nanobody (Gluebody) G3-052:
3.6.4.12;

Protein crystallography data

The structure of Crystal Structure of Human RECQL5 Helicase Apo Form in Complex with Engineered Nanobody (Gluebody) G3-052, PDB code: 7zmo 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) 100.67 / 3.75
Space group P 2 21 21
Cell size a, b, c (Å), α, β, γ (°) 89.517, 150.87, 269.342, 90, 90, 90
R / Rfree (%) 28.3 / 30.6

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Human RECQL5 Helicase Apo Form in Complex with Engineered Nanobody (Gluebody) G3-052 (pdb code 7zmo). 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) G3-052, PDB code: 7zmo:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 7zmo

Go back to Zinc Binding Sites List in 7zmo
Zinc binding site 1 out of 2 in the Crystal Structure of Human RECQL5 Helicase Apo Form in Complex with Engineered Nanobody (Gluebody) G3-052


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) G3-052 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn501

b:141.6
occ:1.00
SG A:CYS434 2.3 170.6 1.0
SG A:CYS427 2.3 118.4 1.0
SG A:CYS431 2.4 143.9 1.0
SG A:CYS411 2.4 94.3 1.0
CB A:CYS434 2.9 179.1 1.0
CB A:CYS431 3.0 143.3 1.0
CB A:CYS427 3.2 119.6 1.0
N A:CYS431 3.5 153.2 1.0
CB A:CYS411 3.7 96.9 1.0
CA A:CYS431 3.8 148.8 1.0
C A:GLY430 4.1 156.4 1.0
CA A:CYS434 4.1 159.1 1.0
CA A:CYS411 4.2 106.9 1.0
N A:CYS434 4.2 139.4 1.0
CD2 A:HIS413 4.3 118.4 1.0
N A:ARG412 4.3 147.7 1.0
C A:CYS431 4.4 156.5 1.0
N A:GLY430 4.5 143.1 1.0
CA A:CYS427 4.5 134.1 1.0
O A:CYS431 4.5 196.2 1.0
O A:GLY430 4.6 204.6 1.0
C A:CYS411 4.6 123.7 1.0
CA A:GLY430 4.7 145.7 1.0
N A:HIS413 4.9 124.2 1.0

Zinc binding site 2 out of 2 in 7zmo

Go back to Zinc Binding Sites List in 7zmo
Zinc binding site 2 out of 2 in the Crystal Structure of Human RECQL5 Helicase Apo Form in Complex with Engineered Nanobody (Gluebody) G3-052


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) G3-052 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn501

b:98.3
occ:1.00
SG B:CYS431 2.2 169.2 1.0
SG B:CYS411 2.3 92.2 1.0
SG B:CYS427 2.5 70.0 1.0
SG B:CYS434 3.0 224.6 1.0
CB B:CYS431 3.1 141.9 1.0
CB B:CYS434 3.2 176.8 1.0
CB B:CYS411 3.3 89.6 1.0
CB B:CYS427 3.5 90.7 1.0
CD2 B:HIS413 3.9 141.5 1.0
N B:CYS431 4.0 144.4 1.0
N B:ARG412 4.0 137.9 1.0
CA B:CYS431 4.0 142.5 1.0
CA B:CYS411 4.1 100.7 1.0
C B:CYS411 4.2 113.6 1.0
N B:HIS413 4.2 126.0 1.0
N B:CYS434 4.3 158.6 1.0
CA B:CYS434 4.3 169.9 1.0
C B:GLY430 4.5 137.1 1.0
CG B:HIS413 4.6 133.2 1.0
CB B:HIS413 4.7 130.4 1.0
C B:CYS431 4.7 150.8 1.0
CA B:CYS427 4.8 112.6 1.0
O B:CYS431 4.8 194.9 1.0
O B:CYS411 4.9 118.5 1.0
O B:GLY430 4.9 159.9 1.0
N B:GLY430 4.9 136.7 1.0
CA B:ARG412 5.0 164.9 1.0
NE2 B:HIS413 5.0 145.4 1.0

Reference:

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.
Page generated: Sat Apr 8 07:09:41 2023

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