Zinc in PDB 7zms: Crystal Structure of Human RECQL5 Helicase Apo Form in Complex with Engineered Nanobody (Gluebody) G4-043

Enzymatic activity of Crystal Structure of Human RECQL5 Helicase Apo Form in Complex with Engineered Nanobody (Gluebody) G4-043

All present enzymatic activity of Crystal Structure of Human RECQL5 Helicase Apo Form in Complex with Engineered Nanobody (Gluebody) G4-043:
3.6.4.12;

Protein crystallography data

The structure of Crystal Structure of Human RECQL5 Helicase Apo Form in Complex with Engineered Nanobody (Gluebody) G4-043, PDB code: 7zms 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) 40.99 / 2.70
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 81.909, 90.121, 216.571, 90, 90, 90
R / Rfree (%) 23.5 / 27.6

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) G4-043 (pdb code 7zms). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of Human RECQL5 Helicase Apo Form in Complex with Engineered Nanobody (Gluebody) G4-043, PDB code: 7zms:

Zinc binding site 1 out of 1 in 7zms

Go back to Zinc Binding Sites List in 7zms
Zinc binding site 1 out of 1 in the Crystal Structure of Human RECQL5 Helicase Apo Form in Complex with Engineered Nanobody (Gluebody) G4-043


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) G4-043 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn501

b:76.9
occ:1.00
 SG A:CYS431 2.2 73.7 1.0
SG A:CYS411 2.3 69.9 1.0
SG A:CYS427 2.3 58.1 1.0
SG A:CYS434 2.6 80.0 1.0
CB A:CYS434 3.0 89.8 1.0
CB A:CYS431 3.2 77.8 1.0
CB A:CYS411 3.3 73.3 1.0
CB A:CYS427 3.5 71.2 1.0
CA A:CYS411 3.5 71.8 1.0
N A:ARG412 3.9 71.2 1.0
N A:CYS431 3.9 71.3 1.0
N A:CYS434 4.0 75.9 1.0
CA A:CYS431 4.0 74.9 1.0
CA A:CYS434 4.0 84.1 1.0
C A:CYS411 4.1 71.8 1.0
CD2 A:HIS413 4.5 76.0 1.0
C A:GLY430 4.6 74.8 1.0
C A:CYS431 4.6 73.9 1.0
O A:CYS431 4.6 72.6 1.0
N A:HIS413 4.7 59.7 1.0
N A:GLY430 4.8 82.4 1.0
CA A:CYS427 4.8 78.5 1.0
N A:CYS411 4.8 76.9 1.0
CB A:HIS413 4.9 61.2 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 07:09:46 2023

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