Zinc in PDB 7zmn: Crystal Structure of Human RECQL5 Helicase Apo Form in Complex with Engineered Nanobody (Gluebody) G3-048

Enzymatic activity of Crystal Structure of Human RECQL5 Helicase Apo Form in Complex with Engineered Nanobody (Gluebody) G3-048

All present enzymatic activity of Crystal Structure of Human RECQL5 Helicase Apo Form in Complex with Engineered Nanobody (Gluebody) G3-048:
3.6.4.12;

Protein crystallography data

The structure of Crystal Structure of Human RECQL5 Helicase Apo Form in Complex with Engineered Nanobody (Gluebody) G3-048, PDB code: 7zmn 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) 129.53 / 3.20
Space group P 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 79.503, 89.573, 259.056, 90, 90, 90
R / Rfree (%) 24.2 / 27.5

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) G3-048 (pdb code 7zmn). 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) G3-048, PDB code: 7zmn:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 7zmn

Go back to Zinc Binding Sites List in 7zmn
Zinc binding site 1 out of 2 in the Crystal Structure of Human RECQL5 Helicase Apo Form in Complex with Engineered Nanobody (Gluebody) G3-048


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) G3-048 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn501

b:89.2
occ:1.00
SG A:CYS411 2.1 75.9 1.0
SG A:CYS431 2.2 83.7 1.0
SG A:CYS427 2.5 46.3 1.0
SG A:CYS434 2.7 77.6 1.0
CB A:CYS411 2.8 78.2 1.0
CA A:CYS411 3.1 77.9 1.0
CB A:CYS434 3.2 89.8 1.0
CB A:CYS431 3.5 83.1 1.0
CB A:CYS427 3.5 50.5 1.0
N A:ARG412 3.6 77.4 1.0
C A:CYS411 3.7 78.4 1.0
N A:CYS434 4.1 78.6 1.0
CA A:CYS434 4.1 86.9 1.0
N A:CYS431 4.2 76.8 1.0
CA A:CYS431 4.3 78.0 1.0
N A:CYS411 4.4 78.3 1.0
N A:HIS413 4.5 74.8 1.0
O A:CYS431 4.8 73.9 1.0
C A:CYS431 4.8 74.8 1.0
C A:GLY430 4.8 72.7 1.0
O A:CYS411 4.8 88.5 1.0
CA A:ARG412 4.9 81.7 1.0
CA A:CYS427 4.9 54.6 1.0
CB A:HIS413 5.0 74.0 1.0

Zinc binding site 2 out of 2 in 7zmn

Go back to Zinc Binding Sites List in 7zmn
Zinc binding site 2 out of 2 in the Crystal Structure of Human RECQL5 Helicase Apo Form in Complex with Engineered Nanobody (Gluebody) G3-048


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) G3-048 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn501

b:70.8
occ:1.00
SG B:CYS411 2.2 52.3 1.0
SG B:CYS431 2.2 85.6 1.0
SG B:CYS427 2.3 48.0 1.0
SG B:CYS434 2.4 92.8 1.0
CB B:CYS411 3.0 61.5 1.0
CB B:CYS434 3.2 93.3 1.0
CB B:CYS431 3.3 81.7 1.0
CB B:CYS427 3.4 54.8 1.0
CA B:CYS411 3.4 67.5 1.0
N B:CYS431 3.9 74.4 1.0
N B:ARG412 3.9 70.5 1.0
C B:CYS411 4.0 68.1 1.0
CA B:CYS431 4.1 79.3 1.0
N B:CYS434 4.1 86.3 1.0
CA B:CYS434 4.2 93.0 1.0
C B:GLY430 4.5 73.8 1.0
O B:CYS431 4.6 70.4 1.0
N B:HIS413 4.6 62.6 1.0
C B:CYS431 4.6 77.1 1.0
N B:CYS411 4.7 76.6 1.0
CA B:CYS427 4.8 60.2 1.0
N B:GLY430 4.9 80.0 1.0
CB B:HIS413 4.9 68.2 1.0
CD2 B:HIS413 4.9 64.2 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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