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Zinc in PDB 7zmq: Crystal Structure of Human RECQL5 Helicase Apo Form in Complex with Engineered Nanobody (Gluebody) G2*-006

Enzymatic activity of Crystal Structure of Human RECQL5 Helicase Apo Form in Complex with Engineered Nanobody (Gluebody) G2*-006

All present enzymatic activity of Crystal Structure of Human RECQL5 Helicase Apo Form in Complex with Engineered Nanobody (Gluebody) G2*-006:
3.6.4.12;

Protein crystallography data

The structure of Crystal Structure of Human RECQL5 Helicase Apo Form in Complex with Engineered Nanobody (Gluebody) G2*-006, PDB code: 7zmq 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) 99.67 / 2.70
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 115.13, 199.086, 174.158, 90, 90, 90
R / Rfree (%) 22.5 / 25.8

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) G2*-006 (pdb code 7zmq). 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) G2*-006, PDB code: 7zmq:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 7zmq

Go back to Zinc Binding Sites List in 7zmq
Zinc binding site 1 out of 2 in the Crystal Structure of Human RECQL5 Helicase Apo Form in Complex with Engineered Nanobody (Gluebody) G2*-006


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) G2*-006 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn501

b:47.7
occ:1.00
SG A:CYS427 2.1 43.6 1.0
SG A:CYS431 2.2 40.0 1.0
SG A:CYS434 2.3 61.0 1.0
SG A:CYS411 2.3 45.4 1.0
CB A:CYS431 3.2 45.1 1.0
CB A:CYS434 3.2 54.8 1.0
CB A:CYS427 3.3 48.9 1.0
CB A:CYS411 3.3 38.3 1.0
CA A:CYS411 3.5 44.1 1.0
N A:CYS431 4.0 34.7 1.0
N A:ARG412 4.0 47.0 1.0
CA A:CYS431 4.1 39.5 1.0
N A:CYS434 4.1 50.3 1.0
C A:CYS411 4.2 49.3 1.0
CA A:CYS434 4.2 55.4 1.0
CD2 A:HIS413 4.4 48.6 1.0
C A:GLY430 4.5 39.1 1.0
O A:CYS431 4.6 41.8 1.0
CA A:CYS427 4.7 45.7 1.0
C A:CYS431 4.7 41.2 1.0
N A:HIS413 4.8 43.6 1.0
N A:CYS411 4.8 44.5 1.0
N A:GLY430 4.8 51.9 1.0
O A:CYS427 4.9 56.2 1.0
O A:GLY430 5.0 33.2 1.0

Zinc binding site 2 out of 2 in 7zmq

Go back to Zinc Binding Sites List in 7zmq
Zinc binding site 2 out of 2 in the Crystal Structure of Human RECQL5 Helicase Apo Form in Complex with Engineered Nanobody (Gluebody) G2*-006


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) G2*-006 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn501

b:56.8
occ:1.00
SG B:CYS411 2.1 53.6 1.0
SG B:CYS427 2.1 42.4 1.0
SG B:CYS434 2.2 60.5 1.0
SG B:CYS431 2.3 49.9 1.0
CB B:CYS411 3.1 47.5 1.0
CB B:CYS427 3.2 48.6 1.0
CB B:CYS434 3.2 59.5 1.0
CB B:CYS431 3.3 49.2 1.0
CA B:CYS411 3.5 51.9 1.0
N B:ARG412 4.0 52.2 1.0
N B:CYS431 4.1 44.0 1.0
N B:CYS434 4.1 51.0 1.0
C B:CYS411 4.2 51.6 1.0
CA B:CYS431 4.2 45.0 1.0
CA B:CYS434 4.2 58.0 1.0
CD2 B:HIS413 4.5 50.5 1.0
C B:GLY430 4.6 49.5 1.0
CA B:CYS427 4.6 51.2 1.0
N B:CYS411 4.7 50.9 1.0
O B:CYS431 4.7 46.7 1.0
C B:CYS431 4.8 45.6 1.0
N B:HIS413 4.8 44.0 1.0
N B:GLY430 4.8 58.0 1.0
O B:CYS427 4.9 56.8 1.0
C B:CYS427 5.0 53.2 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: Wed Oct 30 17:10:42 2024

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